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Protein

Heme-binding protein 2

Gene

HEBP2

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

Functioni

Can promote mitochondrial permeability transition and facilitate necrotic cell death under different types of stress conditions. Does not bind hemin.1 Publication

GO - Biological processi

  • negative regulation of mitochondrial membrane potential Source: UniProtKB
  • positive regulation of mitochondrial membrane permeability Source: UniProtKB
  • positive regulation of necrotic cell death Source: UniProtKB
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Heme-binding protein 2
Alternative name(s):
Placental protein 23
Short name:
PP23
Protein SOUL
Gene namesi
Name:HEBP2
Synonyms:C6orf34, SOUL
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:15716. HEBP2.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • mitochondrion Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA25935.

Polymorphism and mutation databases

BioMutaiHEBP2.
DMDMi74753513.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 205204Heme-binding protein 2PRO_0000116900Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources
Modified residuei181 – 1811PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9Y5Z4.
MaxQBiQ9Y5Z4.
PaxDbiQ9Y5Z4.
PeptideAtlasiQ9Y5Z4.
PRIDEiQ9Y5Z4.

PTM databases

iPTMnetiQ9Y5Z4.
PhosphoSiteiQ9Y5Z4.

Expressioni

Tissue specificityi

Detected in placenta.1 Publication

Gene expression databases

BgeeiENSG00000051620.
CleanExiHS_HEBP2.
ExpressionAtlasiQ9Y5Z4. baseline and differential.
GenevisibleiQ9Y5Z4. HS.

Organism-specific databases

HPAiHPA016928.

Interactioni

Subunit structurei

Monomer. Interacts with LRPPRC. May interact with BCL2L1. An interaction with BCL2L1 was observed using a peptide, but not with the full-length protein. The full-length protein would have to undergo a major conformation change for the interaction to occur.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PDCD6O753404EBI-741593,EBI-352915

Protein-protein interaction databases

BioGridi117128. 4 interactions.
IntActiQ9Y5Z4. 2 interactions.
STRINGi9606.ENSP00000058691.

Structurei

Secondary structure

1
205
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi29 – 313Combined sources
Turni35 – 373Combined sources
Beta strandi39 – 435Combined sources
Beta strandi46 – 5611Combined sources
Helixi58 – 7316Combined sources
Beta strandi89 – 946Combined sources
Beta strandi97 – 1015Combined sources
Beta strandi103 – 1108Combined sources
Helixi113 – 1164Combined sources
Beta strandi122 – 1243Combined sources
Beta strandi127 – 1326Combined sources
Beta strandi135 – 14410Combined sources
Helixi148 – 16417Combined sources
Beta strandi174 – 18310Combined sources
Beta strandi186 – 1883Combined sources
Beta strandi190 – 1967Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3R85X-ray1.95E/F/G/H147-172[»]
3R8JX-ray1.60A/B2-205[»]
3R8KX-ray2.85A/B/C/D2-205[»]
4AYZX-ray3.50A/B1-205[»]
4B0YX-ray3.50A1-205[»]
ProteinModelPortaliQ9Y5Z4.
SMRiQ9Y5Z4. Positions 19-198.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

Forms a distorted beta-barrel structure, with two helices that are packed against the outer surface of the barrel.1 Publication

Sequence similaritiesi

Belongs to the HEBP family.Curated

Phylogenomic databases

eggNOGiENOG410IZTQ. Eukaryota.
ENOG410ZWW6. LUCA.
GeneTreeiENSGT00530000063312.
HOVERGENiHBG097982.
InParanoidiQ9Y5Z4.
OMAiFCESSFT.
OrthoDBiEOG091G0ZIG.
PhylomeDBiQ9Y5Z4.
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.

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9Y5Z4-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAEPLQPDPG AAEDAAAQAV ETPGWKAPED AGPQPGSYEI RHYGPAKWVS
60 70 80 90 100
TSVESMDWDS AIQTGFTKLN SYIQGKNEKE MKIKMTAPVT SYVEPGSGPF
110 120 130 140 150
SESTITISLY IPSEQQFDPP RPLESDVFIE DRAEMTVFVR SFDGFSSAQK
160 170 180 190 200
NQEQLLTLAS ILREDGKVFD EKVYYTAGYN SPVKLLNRNN EVWLIQKNEP

TKENE
Length:205
Mass (Da):22,875
Last modified:November 1, 1999 - v1
Checksum:iA0B5131F94783E07
GO
Isoform 2 (identifier: Q9Y5Z4-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     12-33: AEDAAAQAVETPGWKAPEDAGP → F

Show »
Length:184
Mass (Da):20,859
Checksum:iE9AD02AF9E32C67B
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti140 – 1401R → Q.
Corresponds to variant rs3734303 [ dbSNP | Ensembl ].
VAR_053364
Natural varianti191 – 1911E → A.
Corresponds to variant rs14812 [ dbSNP | Ensembl ].
VAR_053365

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei12 – 3322AEDAA…EDAGP → F in isoform 2. 1 PublicationVSP_017057Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF117616 mRNA. Translation: AAD32099.1.
AF411610 mRNA. Translation: AAL07394.1.
AY427823 mRNA. Translation: AAR88624.1.
AL031003 Genomic DNA. Translation: CAI20539.1.
BC008205 mRNA. Translation: AAH08205.1.
BC010290 mRNA. Translation: AAH10290.1.
BC093037 mRNA. Translation: AAH93037.1.
CCDSiCCDS5191.1. [Q9Y5Z4-1]
RefSeqiNP_055135.1. NM_014320.2. [Q9Y5Z4-1]
UniGeneiHs.486589.

Genome annotation databases

EnsembliENST00000607197; ENSP00000475750; ENSG00000051620. [Q9Y5Z4-1]
GeneIDi23593.
KEGGihsa:23593.
UCSCiuc003qhw.2. human. [Q9Y5Z4-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF117616 mRNA. Translation: AAD32099.1.
AF411610 mRNA. Translation: AAL07394.1.
AY427823 mRNA. Translation: AAR88624.1.
AL031003 Genomic DNA. Translation: CAI20539.1.
BC008205 mRNA. Translation: AAH08205.1.
BC010290 mRNA. Translation: AAH10290.1.
BC093037 mRNA. Translation: AAH93037.1.
CCDSiCCDS5191.1. [Q9Y5Z4-1]
RefSeqiNP_055135.1. NM_014320.2. [Q9Y5Z4-1]
UniGeneiHs.486589.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3R85X-ray1.95E/F/G/H147-172[»]
3R8JX-ray1.60A/B2-205[»]
3R8KX-ray2.85A/B/C/D2-205[»]
4AYZX-ray3.50A/B1-205[»]
4B0YX-ray3.50A1-205[»]
ProteinModelPortaliQ9Y5Z4.
SMRiQ9Y5Z4. Positions 19-198.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117128. 4 interactions.
IntActiQ9Y5Z4. 2 interactions.
STRINGi9606.ENSP00000058691.

PTM databases

iPTMnetiQ9Y5Z4.
PhosphoSiteiQ9Y5Z4.

Polymorphism and mutation databases

BioMutaiHEBP2.
DMDMi74753513.

Proteomic databases

EPDiQ9Y5Z4.
MaxQBiQ9Y5Z4.
PaxDbiQ9Y5Z4.
PeptideAtlasiQ9Y5Z4.
PRIDEiQ9Y5Z4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000607197; ENSP00000475750; ENSG00000051620. [Q9Y5Z4-1]
GeneIDi23593.
KEGGihsa:23593.
UCSCiuc003qhw.2. human. [Q9Y5Z4-1]

Organism-specific databases

CTDi23593.
GeneCardsiHEBP2.
HGNCiHGNC:15716. HEBP2.
HPAiHPA016928.
MIMi605825. gene.
neXtProtiNX_Q9Y5Z4.
PharmGKBiPA25935.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IZTQ. Eukaryota.
ENOG410ZWW6. LUCA.
GeneTreeiENSGT00530000063312.
HOVERGENiHBG097982.
InParanoidiQ9Y5Z4.
OMAiFCESSFT.
OrthoDBiEOG091G0ZIG.
PhylomeDBiQ9Y5Z4.
TreeFamiTF328887.

Miscellaneous databases

ChiTaRSiHEBP2. human.
GeneWikiiHEBP2.
GenomeRNAii23593.
PROiQ9Y5Z4.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000051620.
CleanExiHS_HEBP2.
ExpressionAtlasiQ9Y5Z4. baseline and differential.
GenevisibleiQ9Y5Z4. 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...

Entry informationi

Entry nameiHEBP2_HUMAN
AccessioniPrimary (citable) accession number: Q9Y5Z4
Secondary accession number(s): Q96P57
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2006
Last sequence update: November 1, 1999
Last modified: September 7, 2016
This is version 120 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

Caution

Has been described as heme-binding protein in mouse, but His-42, a residue essential for heme binding in mouse, is not conserved in all orthologs, or in the heme-binding family member HEBP1.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: 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.