HEBP1_HUMAN
ID HEBP1_HUMAN Reviewed; 189 AA.
AC Q9NRV9; A8K1G2; Q9Y5Z5;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 152.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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 two-
RT tissue suppression subtractive hybridization and database searches.";
RL Brain Res. Mol. Brain Res. 74:175-181(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND 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 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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., 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 project:
RT 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., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: May bind free porphyrinogens that may be present in the cell
CC and thus facilitate removal of these potentially toxic compound. Binds
CC with a high affinity to one molecule of heme or porphyrins. It binds
CC metalloporphyrins, free porphyrins and N-methylprotoporphyrin with
CC similar affinities. {ECO:0000269|PubMed:12413491}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:12413491}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12413491}.
CC -!- DOMAIN: Forms a distorted beta-barrel structure, with two helices that
CC are packed against the outer surface of the barrel. Porphyrins are
CC expected to bind to a hydrophobic patch on the outer surface of the
CC beta-barrel structure (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the HEBP family. {ECO:0000305}.
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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 CCDS; CCDS31749.1; -.
DR RefSeq; NP_057071.2; NM_015987.4.
DR AlphaFoldDB; Q9NRV9; -.
DR SMR; Q9NRV9; -.
DR BioGRID; 119164; 19.
DR IntAct; Q9NRV9; 7.
DR STRING; 9606.ENSP00000014930; -.
DR iPTMnet; Q9NRV9; -.
DR MetOSite; Q9NRV9; -.
DR PhosphoSitePlus; Q9NRV9; -.
DR BioMuta; HEBP1; -.
DR DMDM; 74734327; -.
DR REPRODUCTION-2DPAGE; IPI00148063; -.
DR EPD; Q9NRV9; -.
DR jPOST; Q9NRV9; -.
DR MassIVE; Q9NRV9; -.
DR MaxQB; Q9NRV9; -.
DR PaxDb; Q9NRV9; -.
DR PeptideAtlas; Q9NRV9; -.
DR PRIDE; Q9NRV9; -.
DR ProteomicsDB; 82426; -.
DR TopDownProteomics; Q9NRV9; -.
DR Antibodypedia; 23570; 169 antibodies from 23 providers.
DR DNASU; 50865; -.
DR Ensembl; ENST00000014930.9; ENSP00000014930.4; ENSG00000013583.10.
DR GeneID; 50865; -.
DR KEGG; hsa:50865; -.
DR MANE-Select; ENST00000014930.9; ENSP00000014930.4; NM_015987.5; NP_057071.2.
DR UCSC; uc001rbd.4; human.
DR CTD; 50865; -.
DR DisGeNET; 50865; -.
DR GeneCards; HEBP1; -.
DR HGNC; HGNC:17176; HEBP1.
DR HPA; ENSG00000013583; Tissue enhanced (intestine).
DR MIM; 605826; gene.
DR neXtProt; NX_Q9NRV9; -.
DR OpenTargets; ENSG00000013583; -.
DR PharmGKB; PA29236; -.
DR VEuPathDB; HostDB:ENSG00000013583; -.
DR eggNOG; ENOG502RYZW; Eukaryota.
DR GeneTree; ENSGT00940000160320; -.
DR HOGENOM; CLU_068699_3_0_1; -.
DR InParanoid; Q9NRV9; -.
DR OMA; MLGMIRN; -.
DR OrthoDB; 1611913at2759; -.
DR PhylomeDB; Q9NRV9; -.
DR TreeFam; TF328887; -.
DR PathwayCommons; Q9NRV9; -.
DR Reactome; R-HSA-418594; G alpha (i) signalling events.
DR Reactome; R-HSA-444473; Formyl peptide receptors bind formyl peptides and many other ligands.
DR SignaLink; Q9NRV9; -.
DR BioGRID-ORCS; 50865; 14 hits in 1080 CRISPR screens.
DR ChiTaRS; HEBP1; human.
DR GenomeRNAi; 50865; -.
DR Pharos; Q9NRV9; Tbio.
DR PRO; PR:Q9NRV9; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q9NRV9; protein.
DR Bgee; ENSG00000013583; Expressed in jejunal mucosa and 203 other tissues.
DR ExpressionAtlas; Q9NRV9; baseline and differential.
DR Genevisible; Q9NRV9; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0020037; F:heme binding; ISS:UniProtKB.
DR GO; GO:0007623; P:circadian rhythm; TAS:ProtInc.
DR Gene3D; 3.20.80.10; -; 1.
DR InterPro; IPR011256; Reg_factor_effector_dom_sf.
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 Cytoplasm; Reference proteome.
FT CHAIN 1..189
FT /note="Heme-binding protein 1"
FT /id="PRO_0000116897"
FT VARIANT 183
FT /note="E -> D (in dbSNP:rs1941)"
FT /id="VAR_053363"
FT CONFLICT 158
FT /note="T -> P (in Ref. 1; AAD32098)"
FT /evidence="ECO:0000305"
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
