Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Heme-binding protein 2

Gene

Hebp2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 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 (By similarity). May have low affinity for heme.By similarity1 Publication

GO - Biological processi

Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Heme-binding protein 2
Alternative name(s):
Protein SOUL
Gene namesi
Name:Hebp2
Synonyms:Soul
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 10

Organism-specific databases

MGIiMGI:1860084. Hebp2.

Subcellular locationi

  • Cytoplasm By similarity
  • Mitochondrion By similarity

  • Note: Mainly localized to the cytoplasm with a much lower abundance in the mitochondrion.By similarity

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm, Mitochondrion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi42 – 421H → A: Loss of heme binding. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 205204Heme-binding protein 2PRO_0000116901Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei181 – 1811PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9WU63.
PaxDbiQ9WU63.
PRIDEiQ9WU63.

PTM databases

PhosphoSiteiQ9WU63.

Expressioni

Gene expression databases

BgeeiQ9WU63.
CleanExiMM_HEBP2.
GenevisibleiQ9WU63. MM.

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 (By similarity).By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000020000.

Structurei

3D structure databases

ProteinModelPortaliQ9WU63.
SMRiQ9WU63. 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.By similarity

Sequence similaritiesi

Belongs to the HEBP family.Curated

Phylogenomic databases

eggNOGiENOG410IZTQ. Eukaryota.
ENOG410ZWW6. LUCA.
GeneTreeiENSGT00530000063312.
HOGENOMiHOG000237638.
HOVERGENiHBG097982.
InParanoidiQ9WU63.
OMAiFCESSFT.
OrthoDBiEOG7B5WZC.
PhylomeDBiQ9WU63.
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.

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

Q9WU63-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAEEPEPDLG VAEGSEDQAL EMPSWKAPED IDPQPGSYEI RHYGPAKWVS
60 70 80 90 100
TCVESLDWDS AIQTGFTKLN GYIQGKNEKE MKIKLTAPVT SYVEPGSSPF
110 120 130 140 150
SESTITISLY IPSEQQPDPP RPSESDVFIE DRAEMTVFVR SFDGFSSGQK
160 170 180 190 200
NQEQLLTLAN ILREEGKVFN EKVFYTAGYS SPFQLLDRNN EVWLIQKNEP

SVENK
Length:205
Mass (Da):23,063
Last modified:November 1, 1999 - v1
Checksum:i821B33F3E77DB05D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF117614 mRNA. Translation: AAD32097.1.
AK078130 mRNA. Translation: BAC37141.1.
CCDSiCCDS23711.1.
RefSeqiNP_062360.1. NM_019487.3.
UniGeneiMm.35551.

Genome annotation databases

EnsembliENSMUST00000020000; ENSMUSP00000020000; ENSMUSG00000019853.
GeneIDi56016.
KEGGimmu:56016.
UCSCiuc007emk.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF117614 mRNA. Translation: AAD32097.1.
AK078130 mRNA. Translation: BAC37141.1.
CCDSiCCDS23711.1.
RefSeqiNP_062360.1. NM_019487.3.
UniGeneiMm.35551.

3D structure databases

ProteinModelPortaliQ9WU63.
SMRiQ9WU63. Positions 19-198.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000020000.

PTM databases

PhosphoSiteiQ9WU63.

Proteomic databases

MaxQBiQ9WU63.
PaxDbiQ9WU63.
PRIDEiQ9WU63.

Protocols and materials databases

DNASUi56016.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000020000; ENSMUSP00000020000; ENSMUSG00000019853.
GeneIDi56016.
KEGGimmu:56016.
UCSCiuc007emk.1. mouse.

Organism-specific databases

CTDi23593.
MGIiMGI:1860084. Hebp2.

Phylogenomic databases

eggNOGiENOG410IZTQ. Eukaryota.
ENOG410ZWW6. LUCA.
GeneTreeiENSGT00530000063312.
HOGENOMiHOG000237638.
HOVERGENiHBG097982.
InParanoidiQ9WU63.
OMAiFCESSFT.
OrthoDBiEOG7B5WZC.
PhylomeDBiQ9WU63.
TreeFamiTF328887.

Miscellaneous databases

PROiQ9WU63.
SOURCEiSearch...

Gene expression databases

BgeeiQ9WU63.
CleanExiMM_HEBP2.
GenevisibleiQ9WU63. MM.

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. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Medulla oblongata.
  3. "SOUL in mouse eyes is a new hexameric heme-binding protein with characteristic optical absorption, resonance Raman spectral, and heme-binding properties."
    Sato E., Sagami I., Uchida T., Sato A., Kitagawa T., Igarashi J., Shimizu T.
    Biochemistry 43:14189-14198(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS HEME-BINDING PROTEIN, MUTAGENESIS OF HIS-42.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain and Testis.

Entry informationi

Entry nameiHEBP2_MOUSE
AccessioniPrimary (citable) accession number: Q9WU63
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2006
Last sequence update: November 1, 1999
Last modified: June 8, 2016
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

Has been described as heme-binding protein (PubMed:15518569) in mouse, but the human protein does not bind hemin. His-42, a residue essential for heme binding in mouse, is not conserved in all orthologs, or in the heme-binding family member HEBP1.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.