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Protein

Heme-binding protein 1

Gene

HEBP1

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

Functioni

May bind free porphyrinogens that may be present in the cell and thus facilitate removal of these potentially toxic compound. Binds with a high affinity to one molecule of heme or porphyrins. It binds metalloporphyrins, free porphyrins and N-methylprotoporphyrin with similar affinities.1 Publication

GO - Molecular functioni

GO - Biological processi

  • circadian rhythm Source: ProtInc
Complete GO annotation...

Enzyme and pathway databases

ReactomeiR-HSA-418594. G alpha (i) signalling events.
R-HSA-444473. Formyl peptide receptors bind formyl peptides and many other ligands.

Names & Taxonomyi

Protein namesi
Recommended name:
Heme-binding protein 1
Alternative name(s):
p22HBP
Gene namesi
Name:HEBP1
Synonyms:HBP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:17176. HEBP1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB-SubCell
  • extracellular exosome Source: UniProtKB
  • extracellular region Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA29236.

Polymorphism and mutation databases

BioMutaiHEBP1.
DMDMi74734327.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 189189Heme-binding protein 1PRO_0000116897Add
BLAST

Proteomic databases

EPDiQ9NRV9.
MaxQBiQ9NRV9.
PaxDbiQ9NRV9.
PeptideAtlasiQ9NRV9.
PRIDEiQ9NRV9.
TopDownProteomicsiQ9NRV9.

2D gel databases

REPRODUCTION-2DPAGEIPI00148063.

PTM databases

iPTMnetiQ9NRV9.
PhosphoSiteiQ9NRV9.

Expressioni

Gene expression databases

BgeeiQ9NRV9.
CleanExiHS_HEBP1.
ExpressionAtlasiQ9NRV9. baseline and differential.
GenevisibleiQ9NRV9. HS.

Organism-specific databases

HPAiHPA056417.

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

BioGridi119164. 6 interactions.
IntActiQ9NRV9. 1 interaction.
MINTiMINT-5002021.
STRINGi9606.ENSP00000014930.

Structurei

3D structure databases

ProteinModelPortaliQ9NRV9.
SMRiQ9NRV9. Positions 1-188.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

Forms a distorted beta-barrel structure, with two helices that are packed against the outer surface of the barrel. Porphyrins are expected to bind to a hydrophobic patch on the outer surface of the beta-barrel structure (By similarity).By similarity

Sequence similaritiesi

Belongs to the HEBP family.Curated

Phylogenomic databases

eggNOGiENOG410IKQ6. Eukaryota.
ENOG4111HGX. LUCA.
GeneTreeiENSGT00530000063312.
HOGENOMiHOG000237638.
HOVERGENiHBG053223.
InParanoidiQ9NRV9.
OMAiEVWLVKT.
OrthoDBiEOG7B5WZC.
PhylomeDBiQ9NRV9.
TreeFamiTF328887.

Family and domain databases

InterProiIPR011256. Reg_factor_effector_dom.
IPR006917. SOUL_haem-bd.
[Graphical view]
PANTHERiPTHR11220. PTHR11220. 1 hit.
PfamiPF04832. SOUL. 1 hit.
[Graphical view]
SUPFAMiSSF55136. SSF55136. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9NRV9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLGMIKNSLF GSVETWPWQV LSKGDKEEVA YEERACEGGK FATVEVTDKP
60 70 80 90 100
VDEALREAMP KVAKYAGGTN DKGIGMGMTV PISFAVFPNE DGSLQKKLKV
110 120 130 140 150
WFRIPNQFQS DPPAPSDKSV KIEEREGITV YSMQFGGYAK EADYVAQATR
160 170 180
LRAALEGTAT YRGDIYFCTG YDPPMKPYGR RNEIWLLKT
Length:189
Mass (Da):21,097
Last modified:October 1, 2000 - v1
Checksum:i6ED12EA91B101B02
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti158 – 1581T → P in AAD32098 (PubMed:10640688).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti183 – 1831E → D.
Corresponds to variant rs1941 [ dbSNP | Ensembl ].
VAR_053363

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF117615 mRNA. Translation: AAD32098.1.
AF167473 mRNA. Translation: AAF89618.1.
BT007294 mRNA. Translation: AAP35958.1.
AK289877 mRNA. Translation: BAF82566.1.
CH471094 Genomic DNA. Translation: EAW96295.1.
BC016277 mRNA. Translation: AAH16277.1.
CCDSiCCDS31749.1.
RefSeqiNP_057071.2. NM_015987.4.
UniGeneiHs.642618.

Genome annotation databases

EnsembliENST00000014930; ENSP00000014930; ENSG00000013583.
GeneIDi50865.
KEGGihsa:50865.
UCSCiuc001rbd.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF117615 mRNA. Translation: AAD32098.1.
AF167473 mRNA. Translation: AAF89618.1.
BT007294 mRNA. Translation: AAP35958.1.
AK289877 mRNA. Translation: BAF82566.1.
CH471094 Genomic DNA. Translation: EAW96295.1.
BC016277 mRNA. Translation: AAH16277.1.
CCDSiCCDS31749.1.
RefSeqiNP_057071.2. NM_015987.4.
UniGeneiHs.642618.

3D structure databases

ProteinModelPortaliQ9NRV9.
SMRiQ9NRV9. Positions 1-188.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119164. 6 interactions.
IntActiQ9NRV9. 1 interaction.
MINTiMINT-5002021.
STRINGi9606.ENSP00000014930.

PTM databases

iPTMnetiQ9NRV9.
PhosphoSiteiQ9NRV9.

Polymorphism and mutation databases

BioMutaiHEBP1.
DMDMi74734327.

2D gel databases

REPRODUCTION-2DPAGEIPI00148063.

Proteomic databases

EPDiQ9NRV9.
MaxQBiQ9NRV9.
PaxDbiQ9NRV9.
PeptideAtlasiQ9NRV9.
PRIDEiQ9NRV9.
TopDownProteomicsiQ9NRV9.

Protocols and materials databases

DNASUi50865.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000014930; ENSP00000014930; ENSG00000013583.
GeneIDi50865.
KEGGihsa:50865.
UCSCiuc001rbd.4. human.

Organism-specific databases

CTDi50865.
GeneCardsiHEBP1.
H-InvDBHIX0171642.
HGNCiHGNC:17176. HEBP1.
HPAiHPA056417.
MIMi605826. gene.
neXtProtiNX_Q9NRV9.
PharmGKBiPA29236.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IKQ6. Eukaryota.
ENOG4111HGX. LUCA.
GeneTreeiENSGT00530000063312.
HOGENOMiHOG000237638.
HOVERGENiHBG053223.
InParanoidiQ9NRV9.
OMAiEVWLVKT.
OrthoDBiEOG7B5WZC.
PhylomeDBiQ9NRV9.
TreeFamiTF328887.

Enzyme and pathway databases

ReactomeiR-HSA-418594. G alpha (i) signalling events.
R-HSA-444473. Formyl peptide receptors bind formyl peptides and many other ligands.

Miscellaneous databases

GenomeRNAii50865.
PROiQ9NRV9.
SOURCEiSearch...

Gene expression databases

BgeeiQ9NRV9.
CleanExiHS_HEBP1.
ExpressionAtlasiQ9NRV9. baseline and differential.
GenevisibleiQ9NRV9. HS.

Family and domain databases

InterProiIPR011256. Reg_factor_effector_dom.
IPR006917. SOUL_haem-bd.
[Graphical view]
PANTHERiPTHR11220. PTHR11220. 1 hit.
PfamiPF04832. SOUL. 1 hit.
[Graphical view]
SUPFAMiSSF55136. SSF55136. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Discovery of a putative heme-binding protein family (SOUL/HBP) by two-tissue suppression subtractive hybridization and database searches."
    Zylka M.J., Reppert S.M.
    Brain Res. Mol. Brain Res. 74:175-181(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Characterization of a human and mouse tetrapyrrole-binding protein."
    Jacob Blackmon B., Dailey T.A., Lianchun X., Dailey H.A.
    Arch. Biochem. Biophys. 407:196-201(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, SUBUNIT.
    Tissue: Liver.
  3. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Caudate nucleus.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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].
    Tissue: Uterus.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiHEBP1_HUMAN
AccessioniPrimary (citable) accession number: Q9NRV9
Secondary accession number(s): A8K1G2, Q9Y5Z5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2006
Last sequence update: October 1, 2000
Last modified: June 8, 2016
This is version 116 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: 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. 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.