Full text data of HEBP1
HEBP1
(HBP)
[Confidence: high (present in two of the MS resources)]
Heme-binding protein 1 (p22HBP)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Heme-binding protein 1 (p22HBP)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00148063
IPI00148063 Heme binding protein 1 binding, circadian rhythm soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
IPI00148063 Heme binding protein 1 binding, circadian rhythm soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
UniProt
Q9NRV9
ID HEBP1_HUMAN Reviewed; 189 AA.
AC Q9NRV9; A8K1G2; Q9Y5Z5;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-OCT-2000, sequence version 1.
DT 22-JAN-2014, entry version 95.
DE RecName: Full=Heme-binding protein 1;
DE AltName: Full=p22HBP;
GN Name=HEBP1; Synonyms=HBP;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10640688; DOI=10.1016/S0169-328X(99)00277-6;
RA Zylka M.J., Reppert S.M.;
RT "Discovery of a putative heme-binding protein family (SOUL/HBP) by
RT two-tissue suppression subtractive hybridization and database
RT searches.";
RL Brain Res. Mol. Brain Res. 74:175-181(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP SUBUNIT.
RC TISSUE=Liver;
RX PubMed=12413491; DOI=10.1016/S0003-9861(02)00471-X;
RA Jacob Blackmon B., Dailey T.A., Lianchun X., Dailey H.A.;
RT "Characterization of a human and mouse tetrapyrrole-binding protein.";
RL Arch. Biochem. Biophys. 407:196-201(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Caudate nucleus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: May bind free porphyrinogens that may be present in the
CC cell and thus facilitate removal of these potentially toxic
CC compound. Binds with a high affinity to one molecule of heme or
CC porphyrins. It binds metalloporphyrins, free porphyrins and N-
CC methylprotoporphyrin with similar affinities.
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- DOMAIN: Forms a distorted beta-barrel structure, with two helices
CC that are packed against the outer surface of the barrel.
CC Porphyrins are expected to bind to a hydrophobic patch on the
CC outer surface of the beta-barrel structure (By similarity).
CC -!- SIMILARITY: Belongs to the HEBP family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF117615; AAD32098.1; -; mRNA.
DR EMBL; AF167473; AAF89618.1; -; mRNA.
DR EMBL; BT007294; AAP35958.1; -; mRNA.
DR EMBL; AK289877; BAF82566.1; -; mRNA.
DR EMBL; CH471094; EAW96295.1; -; Genomic_DNA.
DR EMBL; BC016277; AAH16277.1; -; mRNA.
DR RefSeq; NP_057071.2; NM_015987.4.
DR UniGene; Hs.642618; -.
DR ProteinModelPortal; Q9NRV9; -.
DR SMR; Q9NRV9; 1-188.
DR IntAct; Q9NRV9; 1.
DR MINT; MINT-5002021; -.
DR STRING; 9606.ENSP00000014930; -.
DR PhosphoSite; Q9NRV9; -.
DR DMDM; 74734327; -.
DR REPRODUCTION-2DPAGE; IPI00148063; -.
DR PaxDb; Q9NRV9; -.
DR PeptideAtlas; Q9NRV9; -.
DR PRIDE; Q9NRV9; -.
DR DNASU; 50865; -.
DR Ensembl; ENST00000014930; ENSP00000014930; ENSG00000013583.
DR GeneID; 50865; -.
DR KEGG; hsa:50865; -.
DR UCSC; uc001rbd.3; human.
DR CTD; 50865; -.
DR GeneCards; GC12M013128; -.
DR H-InvDB; HIX0171642; -.
DR HGNC; HGNC:17176; HEBP1.
DR HPA; HPA056417; -.
DR MIM; 605826; gene.
DR neXtProt; NX_Q9NRV9; -.
DR PharmGKB; PA29236; -.
DR eggNOG; NOG80843; -.
DR HOGENOM; HOG000237638; -.
DR HOVERGEN; HBG053223; -.
DR InParanoid; Q9NRV9; -.
DR OMA; EVWLVKT; -.
DR OrthoDB; EOG7B5WZC; -.
DR PhylomeDB; Q9NRV9; -.
DR Reactome; REACT_111102; Signal Transduction.
DR GenomeRNAi; 50865; -.
DR NextBio; 53375; -.
DR PRO; PR:Q9NRV9; -.
DR ArrayExpress; Q9NRV9; -.
DR Bgee; Q9NRV9; -.
DR CleanEx; HS_HEBP1; -.
DR Genevestigator; Q9NRV9; -.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0020037; F:heme binding; ISS:UniProtKB.
DR GO; GO:0007623; P:circadian rhythm; TAS:ProtInc.
DR InterPro; IPR011256; Reg_factor_effector_dom.
DR InterPro; IPR006917; SOUL_haem-bd.
DR PANTHER; PTHR11220; PTHR11220; 1.
DR Pfam; PF04832; SOUL; 1.
DR SUPFAM; SSF55136; SSF55136; 1.
PE 1: Evidence at protein level;
KW Complete proteome; Cytoplasm; Polymorphism; Reference proteome.
FT CHAIN 1 189 Heme-binding protein 1.
FT /FTId=PRO_0000116897.
FT VARIANT 183 183 E -> D (in dbSNP:rs1941).
FT /FTId=VAR_053363.
FT CONFLICT 158 158 T -> P (in Ref. 1; AAD32098).
SQ SEQUENCE 189 AA; 21097 MW; 6ED12EA91B101B02 CRC64;
MLGMIKNSLF GSVETWPWQV LSKGDKEEVA YEERACEGGK FATVEVTDKP VDEALREAMP
KVAKYAGGTN DKGIGMGMTV PISFAVFPNE DGSLQKKLKV WFRIPNQFQS DPPAPSDKSV
KIEEREGITV YSMQFGGYAK EADYVAQATR LRAALEGTAT YRGDIYFCTG YDPPMKPYGR
RNEIWLLKT
//
ID HEBP1_HUMAN Reviewed; 189 AA.
AC Q9NRV9; A8K1G2; Q9Y5Z5;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-OCT-2000, sequence version 1.
DT 22-JAN-2014, entry version 95.
DE RecName: Full=Heme-binding protein 1;
DE AltName: Full=p22HBP;
GN Name=HEBP1; Synonyms=HBP;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10640688; DOI=10.1016/S0169-328X(99)00277-6;
RA Zylka M.J., Reppert S.M.;
RT "Discovery of a putative heme-binding protein family (SOUL/HBP) by
RT two-tissue suppression subtractive hybridization and database
RT searches.";
RL Brain Res. Mol. Brain Res. 74:175-181(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP SUBUNIT.
RC TISSUE=Liver;
RX PubMed=12413491; DOI=10.1016/S0003-9861(02)00471-X;
RA Jacob Blackmon B., Dailey T.A., Lianchun X., Dailey H.A.;
RT "Characterization of a human and mouse tetrapyrrole-binding protein.";
RL Arch. Biochem. Biophys. 407:196-201(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Caudate nucleus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: May bind free porphyrinogens that may be present in the
CC cell and thus facilitate removal of these potentially toxic
CC compound. Binds with a high affinity to one molecule of heme or
CC porphyrins. It binds metalloporphyrins, free porphyrins and N-
CC methylprotoporphyrin with similar affinities.
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- DOMAIN: Forms a distorted beta-barrel structure, with two helices
CC that are packed against the outer surface of the barrel.
CC Porphyrins are expected to bind to a hydrophobic patch on the
CC outer surface of the beta-barrel structure (By similarity).
CC -!- SIMILARITY: Belongs to the HEBP family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF117615; AAD32098.1; -; mRNA.
DR EMBL; AF167473; AAF89618.1; -; mRNA.
DR EMBL; BT007294; AAP35958.1; -; mRNA.
DR EMBL; AK289877; BAF82566.1; -; mRNA.
DR EMBL; CH471094; EAW96295.1; -; Genomic_DNA.
DR EMBL; BC016277; AAH16277.1; -; mRNA.
DR RefSeq; NP_057071.2; NM_015987.4.
DR UniGene; Hs.642618; -.
DR ProteinModelPortal; Q9NRV9; -.
DR SMR; Q9NRV9; 1-188.
DR IntAct; Q9NRV9; 1.
DR MINT; MINT-5002021; -.
DR STRING; 9606.ENSP00000014930; -.
DR PhosphoSite; Q9NRV9; -.
DR DMDM; 74734327; -.
DR REPRODUCTION-2DPAGE; IPI00148063; -.
DR PaxDb; Q9NRV9; -.
DR PeptideAtlas; Q9NRV9; -.
DR PRIDE; Q9NRV9; -.
DR DNASU; 50865; -.
DR Ensembl; ENST00000014930; ENSP00000014930; ENSG00000013583.
DR GeneID; 50865; -.
DR KEGG; hsa:50865; -.
DR UCSC; uc001rbd.3; human.
DR CTD; 50865; -.
DR GeneCards; GC12M013128; -.
DR H-InvDB; HIX0171642; -.
DR HGNC; HGNC:17176; HEBP1.
DR HPA; HPA056417; -.
DR MIM; 605826; gene.
DR neXtProt; NX_Q9NRV9; -.
DR PharmGKB; PA29236; -.
DR eggNOG; NOG80843; -.
DR HOGENOM; HOG000237638; -.
DR HOVERGEN; HBG053223; -.
DR InParanoid; Q9NRV9; -.
DR OMA; EVWLVKT; -.
DR OrthoDB; EOG7B5WZC; -.
DR PhylomeDB; Q9NRV9; -.
DR Reactome; REACT_111102; Signal Transduction.
DR GenomeRNAi; 50865; -.
DR NextBio; 53375; -.
DR PRO; PR:Q9NRV9; -.
DR ArrayExpress; Q9NRV9; -.
DR Bgee; Q9NRV9; -.
DR CleanEx; HS_HEBP1; -.
DR Genevestigator; Q9NRV9; -.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0020037; F:heme binding; ISS:UniProtKB.
DR GO; GO:0007623; P:circadian rhythm; TAS:ProtInc.
DR InterPro; IPR011256; Reg_factor_effector_dom.
DR InterPro; IPR006917; SOUL_haem-bd.
DR PANTHER; PTHR11220; PTHR11220; 1.
DR Pfam; PF04832; SOUL; 1.
DR SUPFAM; SSF55136; SSF55136; 1.
PE 1: Evidence at protein level;
KW Complete proteome; Cytoplasm; Polymorphism; Reference proteome.
FT CHAIN 1 189 Heme-binding protein 1.
FT /FTId=PRO_0000116897.
FT VARIANT 183 183 E -> D (in dbSNP:rs1941).
FT /FTId=VAR_053363.
FT CONFLICT 158 158 T -> P (in Ref. 1; AAD32098).
SQ SEQUENCE 189 AA; 21097 MW; 6ED12EA91B101B02 CRC64;
MLGMIKNSLF GSVETWPWQV LSKGDKEEVA YEERACEGGK FATVEVTDKP VDEALREAMP
KVAKYAGGTN DKGIGMGMTV PISFAVFPNE DGSLQKKLKV WFRIPNQFQS DPPAPSDKSV
KIEEREGITV YSMQFGGYAK EADYVAQATR LRAALEGTAT YRGDIYFCTG YDPPMKPYGR
RNEIWLLKT
//
MIM
605826
*RECORD*
*FIELD* NO
605826
*FIELD* TI
*605826 HEME-BINDING PROTEIN 1; HEBP1
;;HBP; HEBP
FPRL2 LIGAND, INCLUDED; F2L, INCLUDED
read more*FIELD* TX
CLONING
By EST database searching for homologs of the chicken Soul gene
(605825), Zylka and Reppert (1999) identified mouse and human cDNAs
encoding HBP and SOUL. Sequence analysis predicted that the 189-amino
acid human HBP protein, which is 80% identical to the mouse sequence,
contains a conserved hydrophobic heme-binding region not found in SOUL.
Northern blot analysis detected a 1.5-kb Hbp transcript in mouse liver.
GENE FUNCTION
By screening organ extracts on cell lines expressing FPRL2 (136539),
Migeotte et al. (2005) isolated F2L (FPRL2 ligand) from spleen. F2L is
an acetylated 21-amino acid peptide derived from the N terminus of
intracellular HBP. F2L bound and activated FPRL2 in the nanomolar range,
triggering intracellular calcium release, inhibition of cAMP
accumulation, and phosphorylation of MAP kinases. Testing on monocytes
and monocyte-derived dendritic cells showed that F2L promoted calcium
mobilization and chemotaxis. Migeotte et al. (2005) concluded that F2L
is a natural chemoattractant peptide for dendritic cells and monocytes
and is specific for FPRL2.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the HEBP
gene to chromosome 12 (TMAP stSG28810).
*FIELD* RF
1. Migeotte, I.; Riboldi, E.; Franssen, J.-D.; Gregoire, F.; Loison,
C.; Wittamer, V.; Detheux, M.; Robberecht, P.; Costagliola, S.; Vassart,
G.; Sozzani, S.; Parmentier, M.; Communi, D.: Identification and
characterization of an endogenous chemotactic ligand specific for
FPRL2. J. Exp. Med. 201: 83-93, 2005.
2. Zylka, M. J.; Reppert, S. M.: Discovery of a putative heme-binding
protein family (SOUL/HBP) by two-tissue suppression subtractive hybridization
and database searches. Molec. Brain Res. 74: 175-181, 1999.
*FIELD* CN
Paul J. Converse - updated: 04/03/2006
*FIELD* CD
Paul J. Converse: 4/6/2001
*FIELD* ED
mgross: 04/03/2006
mgross: 11/27/2001
mgross: 4/6/2001
*RECORD*
*FIELD* NO
605826
*FIELD* TI
*605826 HEME-BINDING PROTEIN 1; HEBP1
;;HBP; HEBP
FPRL2 LIGAND, INCLUDED; F2L, INCLUDED
read more*FIELD* TX
CLONING
By EST database searching for homologs of the chicken Soul gene
(605825), Zylka and Reppert (1999) identified mouse and human cDNAs
encoding HBP and SOUL. Sequence analysis predicted that the 189-amino
acid human HBP protein, which is 80% identical to the mouse sequence,
contains a conserved hydrophobic heme-binding region not found in SOUL.
Northern blot analysis detected a 1.5-kb Hbp transcript in mouse liver.
GENE FUNCTION
By screening organ extracts on cell lines expressing FPRL2 (136539),
Migeotte et al. (2005) isolated F2L (FPRL2 ligand) from spleen. F2L is
an acetylated 21-amino acid peptide derived from the N terminus of
intracellular HBP. F2L bound and activated FPRL2 in the nanomolar range,
triggering intracellular calcium release, inhibition of cAMP
accumulation, and phosphorylation of MAP kinases. Testing on monocytes
and monocyte-derived dendritic cells showed that F2L promoted calcium
mobilization and chemotaxis. Migeotte et al. (2005) concluded that F2L
is a natural chemoattractant peptide for dendritic cells and monocytes
and is specific for FPRL2.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the HEBP
gene to chromosome 12 (TMAP stSG28810).
*FIELD* RF
1. Migeotte, I.; Riboldi, E.; Franssen, J.-D.; Gregoire, F.; Loison,
C.; Wittamer, V.; Detheux, M.; Robberecht, P.; Costagliola, S.; Vassart,
G.; Sozzani, S.; Parmentier, M.; Communi, D.: Identification and
characterization of an endogenous chemotactic ligand specific for
FPRL2. J. Exp. Med. 201: 83-93, 2005.
2. Zylka, M. J.; Reppert, S. M.: Discovery of a putative heme-binding
protein family (SOUL/HBP) by two-tissue suppression subtractive hybridization
and database searches. Molec. Brain Res. 74: 175-181, 1999.
*FIELD* CN
Paul J. Converse - updated: 04/03/2006
*FIELD* CD
Paul J. Converse: 4/6/2001
*FIELD* ED
mgross: 04/03/2006
mgross: 11/27/2001
mgross: 4/6/2001