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Q99797

- MIPEP_HUMAN

UniProt

Q99797 - MIPEP_HUMAN

Protein

Mitochondrial intermediate peptidase

Gene

MIPEP

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 126 (01 Oct 2014)
      Sequence version 2 (26 Feb 2008)
      Previous versions | rss
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    Functioni

    Cleaves proteins, imported into the mitochondrion, to their mature size.

    Catalytic activityi

    Release of an N-terminal octapeptide as second stage of processing of some proteins imported into the mitochondrion.

    Cofactori

    Binds 1 zinc ion.By similarity

    Enzyme regulationi

    Activity is divalent cation-dependent. It is stimulated by manganese, magnesium or calcium ions and reversibly inhibited by zinc, cobalt and iron By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi495 – 4951Zinc; catalyticPROSITE-ProRule annotation
    Active sitei496 – 4961PROSITE-ProRule annotation
    Metal bindingi499 – 4991Zinc; catalyticPROSITE-ProRule annotation
    Metal bindingi502 – 5021Zinc; catalyticPROSITE-ProRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

    1. protein processing involved in protein targeting to mitochondrion Source: ProtInc

    Keywords - Molecular functioni

    Hydrolase, Metalloprotease, Protease

    Keywords - Ligandi

    Calcium, Cobalt, Iron, Magnesium, Manganese, Metal-binding, Zinc

    Protein family/group databases

    MEROPSiM03.A05.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Mitochondrial intermediate peptidase (EC:3.4.24.59)
    Short name:
    MIP
    Gene namesi
    Name:MIPEP
    Synonyms:MIP
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 13

    Organism-specific databases

    HGNCiHGNC:7104. MIPEP.

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrial matrix Source: UniProtKB-SubCell
    2. mitochondrion Source: HPA

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA30822.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 3535MitochondrionAdd
    BLAST
    Chaini36 – 713678Mitochondrial intermediate peptidasePRO_0000028579Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei126 – 1261N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ99797.
    PaxDbiQ99797.
    PRIDEiQ99797.

    PTM databases

    PhosphoSiteiQ99797.

    Expressioni

    Gene expression databases

    ArrayExpressiQ99797.
    BgeeiQ99797.
    CleanExiHS_MIP.
    HS_MIPEP.
    GenevestigatoriQ99797.

    Organism-specific databases

    HPAiHPA030676.
    HPA031669.
    HPA031670.

    Interactioni

    Subunit structurei

    Monomer.By similarity

    Protein-protein interaction databases

    BioGridi110431. 6 interactions.
    IntActiQ99797. 4 interactions.
    MINTiMINT-2815808.
    STRINGi9606.ENSP00000371607.

    Structurei

    3D structure databases

    ProteinModelPortaliQ99797.
    SMRiQ99797. Positions 120-694.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase M3 family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0339.
    HOGENOMiHOG000230535.
    HOVERGENiHBG008215.
    InParanoidiQ99797.
    KOiK01410.
    OMAiLQVFYSA.
    OrthoDBiEOG7TTQ72.
    PhylomeDBiQ99797.
    TreeFamiTF105715.

    Family and domain databases

    Gene3Di1.10.1370.10. 2 hits.
    1.20.1050.40. 1 hit.
    3.40.390.10. 1 hit.
    InterProiIPR024079. MetalloPept_cat_dom.
    IPR024077. Neurolysin/TOP_dom2.
    IPR024080. Neurolysin/TOP_N.
    IPR001567. Pept_M3A_M3B.
    [Graphical view]
    PfamiPF01432. Peptidase_M3. 1 hit.
    [Graphical view]
    PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q99797-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLCVGRLGGL GARAAALPPR RAGRGSLEAG IRARRVSTSW SPVGAAFNVK    50
    PQGSRLDLFG ERRGLFGVPE LSAPEGFHIA QEKALRKTEL LVDRACSTPP 100
    GPQTVLIFDE LSDSLCRVAD LADFVKIAHP EPAFREAAEE ACRSIGTMVE 150
    KLNTNVDLYQ SLQKLLADKK LVDSLDPETR RVAELFMFDF EISGIHLDKE 200
    KRKRAVDLNV KILDLSSTFL MGTNFPNKIE KHLLPEHIRR NFTSAGDHII 250
    IDGLHAESPD DLVREAAYKI FLYPNAGQLK CLEELLSSRD LLAKLVGYST 300
    FSHRALQGTI AKNPETVMQF LEKLSDKLSE RTLKDFEMIR GMKMKLNPQN 350
    SEVMPWDPPY YSGVIRAERY NIEPSLYCPF FSLGACMEGL NILLNRLLGI 400
    SLYAEQPAKG EVWSEDVRKL AVVHESEGLL GYIYCDFFQR ADKPHQDCHF 450
    TIRGGRLKED GDYQLPVVVL MLNLPRSSRS SPTLLTPSMM ENLFHEMGHA 500
    MHSMLGRTRY QHVTGTRCPT DFAEVPSILM EYFANDYRVV NQFARHYQTG 550
    QPLPKNMVSR LCESKKVCAA ADMQLQVFYA TLDQIYHGKH PLRNSTTDIL 600
    KETQEKFYGL PYVPNTAWQL RFSHLVGYGA RYYSYLMSRA VASMVWKECF 650
    LQDPFNRAAG ERYRREMLAH GGGREPMLMV EGMLQKCPSV DDFVSALVSD 700
    LDLDFETFLM DSE 713
    Length:713
    Mass (Da):80,641
    Last modified:February 26, 2008 - v2
    Checksum:i9DBB26B74355B9C1
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti63 – 642RG → AR in AAC51231. (PubMed:9073519)Curated
    Sequence conflicti200 – 2001E → Q in AAC51231. (PubMed:9073519)Curated
    Sequence conflicti348 – 3481P → A in AAC51231. (PubMed:9073519)Curated
    Sequence conflicti467 – 4671V → L in AAC51231. (PubMed:9073519)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti137 – 1371A → V.
    Corresponds to variant rs2312296 [ dbSNP | Ensembl ].
    VAR_038934
    Natural varianti340 – 3401R → Q.
    Corresponds to variant rs11551114 [ dbSNP | Ensembl ].
    VAR_038935
    Natural varianti453 – 4531R → H.
    Corresponds to variant rs12858248 [ dbSNP | Ensembl ].
    VAR_038936
    Natural varianti488 – 4881S → G.3 Publications
    Corresponds to variant rs7333040 [ dbSNP | Ensembl ].
    VAR_038937

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U80034 mRNA. Translation: AAC51231.1.
    AK291923 mRNA. Translation: BAF84612.1.
    AL157368, AL139080, AL445985 Genomic DNA. Translation: CAI15091.1.
    AL139080, AL157368, AL445985 Genomic DNA. Translation: CAI39630.1.
    AL445985, AL139080, AL157368 Genomic DNA. Translation: CAM20040.1.
    BC009934 mRNA. Translation: AAH09934.1.
    CCDSiCCDS9303.1.
    RefSeqiNP_005923.2. NM_005932.3.
    UniGeneiHs.507498.

    Genome annotation databases

    EnsembliENST00000382172; ENSP00000371607; ENSG00000027001.
    GeneIDi4285.
    KEGGihsa:4285.
    UCSCiuc001uox.4. human.

    Polymorphism databases

    DMDMi182639267.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U80034 mRNA. Translation: AAC51231.1 .
    AK291923 mRNA. Translation: BAF84612.1 .
    AL157368 , AL139080 , AL445985 Genomic DNA. Translation: CAI15091.1 .
    AL139080 , AL157368 , AL445985 Genomic DNA. Translation: CAI39630.1 .
    AL445985 , AL139080 , AL157368 Genomic DNA. Translation: CAM20040.1 .
    BC009934 mRNA. Translation: AAH09934.1 .
    CCDSi CCDS9303.1.
    RefSeqi NP_005923.2. NM_005932.3.
    UniGenei Hs.507498.

    3D structure databases

    ProteinModelPortali Q99797.
    SMRi Q99797. Positions 120-694.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110431. 6 interactions.
    IntActi Q99797. 4 interactions.
    MINTi MINT-2815808.
    STRINGi 9606.ENSP00000371607.

    Protein family/group databases

    MEROPSi M03.A05.

    PTM databases

    PhosphoSitei Q99797.

    Polymorphism databases

    DMDMi 182639267.

    Proteomic databases

    MaxQBi Q99797.
    PaxDbi Q99797.
    PRIDEi Q99797.

    Protocols and materials databases

    DNASUi 4285.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000382172 ; ENSP00000371607 ; ENSG00000027001 .
    GeneIDi 4285.
    KEGGi hsa:4285.
    UCSCi uc001uox.4. human.

    Organism-specific databases

    CTDi 4285.
    GeneCardsi GC13M024304.
    HGNCi HGNC:7104. MIPEP.
    HPAi HPA030676.
    HPA031669.
    HPA031670.
    MIMi 602241. gene.
    neXtProti NX_Q99797.
    PharmGKBi PA30822.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0339.
    HOGENOMi HOG000230535.
    HOVERGENi HBG008215.
    InParanoidi Q99797.
    KOi K01410.
    OMAi LQVFYSA.
    OrthoDBi EOG7TTQ72.
    PhylomeDBi Q99797.
    TreeFami TF105715.

    Miscellaneous databases

    ChiTaRSi MIPEP. human.
    GenomeRNAii 4285.
    NextBioi 16857.
    PROi Q99797.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q99797.
    Bgeei Q99797.
    CleanExi HS_MIP.
    HS_MIPEP.
    Genevestigatori Q99797.

    Family and domain databases

    Gene3Di 1.10.1370.10. 2 hits.
    1.20.1050.40. 1 hit.
    3.40.390.10. 1 hit.
    InterProi IPR024079. MetalloPept_cat_dom.
    IPR024077. Neurolysin/TOP_dom2.
    IPR024080. Neurolysin/TOP_N.
    IPR001567. Pept_M3A_M3B.
    [Graphical view ]
    Pfami PF01432. Peptidase_M3. 1 hit.
    [Graphical view ]
    PROSITEi PS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning, expression, and chromosomal assignment of the human mitochondrial intermediate peptidase gene (MIPEP)."
      Chew A., Buck E.A., Peretz S., Sirugo G., Rinaldo P., Isaya G.
      Genomics 40:493-496(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT GLY-488.
      Tissue: Liver.
    2. "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], VARIANT GLY-488.
    3. "The DNA sequence and analysis of human chromosome 13."
      Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
      Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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], VARIANT GLY-488.
      Tissue: Uterus.
    5. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-126, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiMIPEP_HUMAN
    AccessioniPrimary (citable) accession number: Q99797
    Secondary accession number(s): Q5JV15, Q5T9Q9, Q96G65
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1999
    Last sequence update: February 26, 2008
    Last modified: October 1, 2014
    This is version 126 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, Reference proteome

    Documents

    1. Human chromosome 13
      Human chromosome 13: 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