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Protein

Mitochondrial-processing peptidase subunit beta

Gene

PMPCB

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

Functioni

Cleaves presequences (transit peptides) from mitochondrial protein precursors.By similarity

Catalytic activityi

Release of N-terminal transit peptides from precursor proteins imported into the mitochondrion, typically with Arg in position P2.

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi101 – 1011ZincPROSITE-ProRule annotation
Active sitei104 – 1041Proton acceptorPROSITE-ProRule annotation
Metal bindingi105 – 1051ZincPROSITE-ProRule annotation
Metal bindingi181 – 1811ZincPROSITE-ProRule annotation

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. metalloendopeptidase activity Source: InterPro

GO - Biological processi

  1. cellular protein metabolic process Source: Reactome
  2. protein targeting to mitochondrion Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_118595. Mitochondrial protein import.
SignaLinkiO75439.

Protein family/group databases

MEROPSiM16.003.

Names & Taxonomyi

Protein namesi
Recommended name:
Mitochondrial-processing peptidase subunit beta (EC:3.4.24.64)
Alternative name(s):
Beta-MPP
P-52
Gene namesi
Name:PMPCB
Synonyms:MPPB
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:9119. PMPCB.

Subcellular locationi

  1. Mitochondrion matrix By similarity

GO - Cellular componenti

  1. mitochondrial inner membrane Source: Ensembl
  2. mitochondrial matrix Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33445.

Polymorphism and mutation databases

BioMutaiPMPCB.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4545Mitochondrion1 PublicationAdd
BLAST
Chaini46 – 489444Mitochondrial-processing peptidase subunit betaPRO_0000026777Add
BLAST

Proteomic databases

MaxQBiO75439.
PaxDbiO75439.
PRIDEiO75439.

PTM databases

PhosphoSiteiO75439.

Expressioni

Gene expression databases

BgeeiO75439.
CleanExiHS_PMPCB.
ExpressionAtlasiO75439. baseline and differential.
GenevestigatoriO75439.

Organism-specific databases

HPAiHPA040674.

Interactioni

Subunit structurei

Heterodimer of alpha and beta subunits.By similarity

Protein-protein interaction databases

BioGridi114889. 22 interactions.
IntActiO75439. 2 interactions.
MINTiMINT-1401899.
STRINGi9606.ENSP00000249269.

Structurei

3D structure databases

ProteinModelPortaliO75439.
SMRiO75439. Positions 50-486.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M16 family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0612.
GeneTreeiENSGT00550000074701.
HOGENOMiHOG000242450.
HOVERGENiHBG006393.
InParanoidiO75439.
KOiK17732.
OrthoDBiEOG74R1QJ.
PhylomeDBiO75439.
TreeFamiTF105032.

Family and domain databases

Gene3Di3.30.830.10. 2 hits.
InterProiIPR011249. Metalloenz_LuxS/M16.
IPR011237. Pept_M16_dom.
IPR011765. Pept_M16_N.
IPR001431. Pept_M16_Zn_BS.
IPR007863. Peptidase_M16_C.
[Graphical view]
PfamiPF00675. Peptidase_M16. 1 hit.
PF05193. Peptidase_M16_C. 1 hit.
[Graphical view]
SUPFAMiSSF63411. SSF63411. 2 hits.
PROSITEiPS00143. INSULINASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

O75439-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAAAARVVL SSAARRRLWG FSESLLIRGA AGRSLYFGEN RLRSTQAATQ
60 70 80 90 100
VVLNVPETRV TCLESGLRVA SEDSGLSTCT VGLWIDAGSR YENEKNNGTA
110 120 130 140 150
HFLEHMAFKG TKKRSQLDLE LEIENMGAHL NAYTSREQTV YYAKAFSKDL
160 170 180 190 200
PRAVEILADI IQNSTLGEAE IERERGVILR EMQEVETNLQ EVVFDYLHAT
210 220 230 240 250
AYQNTALGRT ILGPTENIKS ISRKDLVDYI TTHYKGPRIV LAAAGGVSHD
260 270 280 290 300
ELLDLAKFHF GDSLCTHKGE IPALPPCKFT GSEIRVRDDK MPLAHLAIAV
310 320 330 340 350
EAVGWAHPDT ICLMVANTLI GNWDRSFGGG MNLSSKLAQL TCHGNLCHSF
360 370 380 390 400
QSFNTSYTDT GLWGLYMVCE SSTVADMLHV VQKEWMRLCT SVTESEVARA
410 420 430 440 450
RNLLKTNMLL QLDGSTPICE DIGRQMLCYN RRIPIPELEA RIDAVNAETI
460 470 480
REVCTKYIYN RSPAIAAVGP IKQLPDFKQI RSNMCWLRD
Length:489
Mass (Da):54,366
Last modified:April 11, 2003 - v2
Checksum:i79250D016E60CFEE
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti16 – 172RR → GG in AAC39915 (PubMed:9653160).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti396 – 3961E → D.
Corresponds to variant rs3087615 [ dbSNP | Ensembl ].
VAR_051572

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF054182 mRNA. Translation: AAC39915.1.
AC004668 Genomic DNA. No translation available.
CCDSiCCDS5730.1.
RefSeqiNP_004270.2. NM_004279.2.
UniGeneiHs.184211.

Genome annotation databases

EnsembliENST00000249269; ENSP00000249269; ENSG00000105819.
GeneIDi9512.
KEGGihsa:9512.
UCSCiuc003vbl.3. human.

Polymorphism and mutation databases

BioMutaiPMPCB.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF054182 mRNA. Translation: AAC39915.1.
AC004668 Genomic DNA. No translation available.
CCDSiCCDS5730.1.
RefSeqiNP_004270.2. NM_004279.2.
UniGeneiHs.184211.

3D structure databases

ProteinModelPortaliO75439.
SMRiO75439. Positions 50-486.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114889. 22 interactions.
IntActiO75439. 2 interactions.
MINTiMINT-1401899.
STRINGi9606.ENSP00000249269.

Protein family/group databases

MEROPSiM16.003.

PTM databases

PhosphoSiteiO75439.

Polymorphism and mutation databases

BioMutaiPMPCB.

Proteomic databases

MaxQBiO75439.
PaxDbiO75439.
PRIDEiO75439.

Protocols and materials databases

DNASUi9512.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000249269; ENSP00000249269; ENSG00000105819.
GeneIDi9512.
KEGGihsa:9512.
UCSCiuc003vbl.3. human.

Organism-specific databases

CTDi9512.
GeneCardsiGC07P102937.
H-InvDBHIX0006969.
HGNCiHGNC:9119. PMPCB.
HPAiHPA040674.
MIMi603131. gene.
neXtProtiNX_O75439.
PharmGKBiPA33445.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0612.
GeneTreeiENSGT00550000074701.
HOGENOMiHOG000242450.
HOVERGENiHBG006393.
InParanoidiO75439.
KOiK17732.
OrthoDBiEOG74R1QJ.
PhylomeDBiO75439.
TreeFamiTF105032.

Enzyme and pathway databases

ReactomeiREACT_118595. Mitochondrial protein import.
SignaLinkiO75439.

Miscellaneous databases

ChiTaRSiPMPCB. human.
GeneWikiiPMPCB.
GenomeRNAii9512.
NextBioi35642.
PROiO75439.
SOURCEiSearch...

Gene expression databases

BgeeiO75439.
CleanExiHS_PMPCB.
ExpressionAtlasiO75439. baseline and differential.
GenevestigatoriO75439.

Family and domain databases

Gene3Di3.30.830.10. 2 hits.
InterProiIPR011249. Metalloenz_LuxS/M16.
IPR011237. Pept_M16_dom.
IPR011765. Pept_M16_N.
IPR001431. Pept_M16_Zn_BS.
IPR007863. Peptidase_M16_C.
[Graphical view]
PfamiPF00675. Peptidase_M16. 1 hit.
PF05193. Peptidase_M16_C. 1 hit.
[Graphical view]
SUPFAMiSSF63411. SSF63411. 2 hits.
PROSITEiPS00143. INSULINASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Identification of genes expressed in human CD34(+) hematopoietic stem/progenitor cells by expressed sequence tags and efficient full-length cDNA cloning."
    Mao M., Fu G., Wu J.-S., Zhang Q.-H., Zhou J., Kan L.-X., Huang Q.-H., He K.-L., Gu B.-W., Han Z.-G., Shen Y., Gu J., Yu Y.-P., Xu S.-H., Wang Y.-X., Chen S.-J., Chen Z.
    Proc. Natl. Acad. Sci. U.S.A. 95:8175-8180(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Umbilical cord blood.
  2. "The DNA sequence of human chromosome 7."
    Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
    , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
    Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "Global profiling of protease cleavage sites by chemoselective labeling of protein N-termini."
    Xu G., Shin S.B., Jaffrey S.R.
    Proc. Natl. Acad. Sci. U.S.A. 106:19310-19315(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE [LARGE SCALE ANALYSIS] OF 46-60.
    Tissue: Leukemic T-cell.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  5. "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.

Entry informationi

Entry nameiMPPB_HUMAN
AccessioniPrimary (citable) accession number: O75439
Secondary accession number(s): O60416, Q96FV4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: April 11, 2003
Last modified: April 29, 2015
This is version 135 of the entry and version 2 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: 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. Peptidase families
    Classification of peptidase families and list of entries
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.