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Q99797 (MIPEP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Mitochondrial intermediate peptidase

Short name=MIP
EC=3.4.24.59
Gene names
Name:MIPEP
Synonyms:MIP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length713 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

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

Cofactor

Binds 1 zinc ion By similarity.

Enzyme regulation

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

Subunit structure

Monomer By similarity.

Subcellular location

Mitochondrion matrix.

Sequence similarities

Belongs to the peptidase M3 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3535Mitochondrion
Chain36 – 713678Mitochondrial intermediate peptidase
PRO_0000028579

Sites

Active site4961 By similarity
Metal binding4951Zinc; catalytic By similarity
Metal binding4991Zinc; catalytic By similarity
Metal binding5021Zinc; catalytic By similarity

Amino acid modifications

Modified residue1261N6-acetyllysine Ref.5

Natural variations

Natural variant1371A → V.
Corresponds to variant rs2312296 [ dbSNP | Ensembl ].
VAR_038934
Natural variant3401R → Q.
Corresponds to variant rs11551114 [ dbSNP | Ensembl ].
VAR_038935
Natural variant4531R → H.
Corresponds to variant rs12858248 [ dbSNP | Ensembl ].
VAR_038936
Natural variant4881S → G. Ref.1 Ref.2 Ref.4
Corresponds to variant rs7333040 [ dbSNP | Ensembl ].
VAR_038937

Experimental info

Sequence conflict63 – 642RG → AR in AAC51231. Ref.1
Sequence conflict2001E → Q in AAC51231. Ref.1
Sequence conflict3481P → A in AAC51231. Ref.1
Sequence conflict4671V → L in AAC51231. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q99797 [UniParc].

Last modified February 26, 2008. Version 2.
Checksum: 9DBB26B74355B9C1

FASTA71380,641
        10         20         30         40         50         60 
MLCVGRLGGL GARAAALPPR RAGRGSLEAG IRARRVSTSW SPVGAAFNVK PQGSRLDLFG 

        70         80         90        100        110        120 
ERRGLFGVPE LSAPEGFHIA QEKALRKTEL LVDRACSTPP GPQTVLIFDE LSDSLCRVAD 

       130        140        150        160        170        180 
LADFVKIAHP EPAFREAAEE ACRSIGTMVE KLNTNVDLYQ SLQKLLADKK LVDSLDPETR 

       190        200        210        220        230        240 
RVAELFMFDF EISGIHLDKE KRKRAVDLNV KILDLSSTFL MGTNFPNKIE KHLLPEHIRR 

       250        260        270        280        290        300 
NFTSAGDHII IDGLHAESPD DLVREAAYKI FLYPNAGQLK CLEELLSSRD LLAKLVGYST 

       310        320        330        340        350        360 
FSHRALQGTI AKNPETVMQF LEKLSDKLSE RTLKDFEMIR GMKMKLNPQN SEVMPWDPPY 

       370        380        390        400        410        420 
YSGVIRAERY NIEPSLYCPF FSLGACMEGL NILLNRLLGI SLYAEQPAKG EVWSEDVRKL 

       430        440        450        460        470        480 
AVVHESEGLL GYIYCDFFQR ADKPHQDCHF TIRGGRLKED GDYQLPVVVL MLNLPRSSRS 

       490        500        510        520        530        540 
SPTLLTPSMM ENLFHEMGHA MHSMLGRTRY QHVTGTRCPT DFAEVPSILM EYFANDYRVV 

       550        560        570        580        590        600 
NQFARHYQTG QPLPKNMVSR LCESKKVCAA ADMQLQVFYA TLDQIYHGKH PLRNSTTDIL 

       610        620        630        640        650        660 
KETQEKFYGL PYVPNTAWQL RFSHLVGYGA RYYSYLMSRA VASMVWKECF LQDPFNRAAG 

       670        680        690        700        710 
ERYRREMLAH GGGREPMLMV EGMLQKCPSV DDFVSALVSD LDLDFETFLM DSE 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_005923.2. NM_005932.3.
UniGeneHs.507498.

3D structure databases

ProteinModelPortalQ99797.
SMRQ99797. Positions 120-694.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110431. 5 interactions.
IntActQ99797. 4 interactions.
MINTMINT-2815808.
STRING9606.ENSP00000371607.

Protein family/group databases

MEROPSM03.A05.

PTM databases

PhosphoSiteQ99797.

Polymorphism databases

DMDM182639267.

Proteomic databases

PaxDbQ99797.
PRIDEQ99797.

Protocols and materials databases

DNASU4285.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000382172; ENSP00000371607; ENSG00000027001.
GeneID4285.
KEGGhsa:4285.
UCSCuc001uox.4. human.

Organism-specific databases

CTD4285.
GeneCardsGC13M024304.
HGNCHGNC:7104. MIPEP.
HPAHPA030676.
HPA031669.
HPA031670.
MIM602241. gene.
neXtProtNX_Q99797.
PharmGKBPA30822.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0339.
HOGENOMHOG000230535.
HOVERGENHBG008215.
InParanoidQ99797.
KOK01410.
OMALQVFYSA.
OrthoDBEOG7TTQ72.
PhylomeDBQ99797.
TreeFamTF105715.

Gene expression databases

ArrayExpressQ99797.
BgeeQ99797.
CleanExHS_MIP.
HS_MIPEP.
GenevestigatorQ99797.

Family and domain databases

Gene3D1.10.1370.10. 2 hits.
1.20.1050.40. 1 hit.
3.40.390.10. 1 hit.
InterProIPR024079. MetalloPept_cat_dom.
IPR024077. Neurolysin/TOP_dom2.
IPR024080. Neurolysin/TOP_N.
IPR001567. Pept_M3A_M3B.
[Graphical view]
PfamPF01432. Peptidase_M3. 1 hit.
[Graphical view]
PROSITEPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMIPEP. human.
GenomeRNAi4285.
NextBio16857.
PROQ99797.
SOURCESearch...

Entry information

Entry nameMIPEP_HUMAN
AccessionPrimary (citable) accession number: Q99797
Secondary accession number(s): Q5JV15, Q5T9Q9, Q96G65
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: February 26, 2008
Last modified: March 19, 2014
This is version 122 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 13

Human chromosome 13: entries, gene names and cross-references to MIM