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Q5JRX3

- PREP_HUMAN

UniProt

Q5JRX3 - PREP_HUMAN

Protein

Presequence protease, mitochondrial

Gene

PITRM1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 97 (01 Oct 2014)
      Sequence version 3 (01 May 2013)
      Previous versions | rss
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    Functioni

    ATP-independent protease that degrades mitochondrial transit peptides after their cleavage. Also degrades other unstructured peptides. Specific for peptides in the range of 10 to 65 residues. Able to degrade amyloid beta A4 (APP) protein when it accumulates in mitochondrion, suggesting a link with Alzheimer disease. Shows a preference for cleavage after small polar residues and before basic residues, but without any positional preference.1 Publication

    Cofactori

    Binds 1 zinc ion per subunit.By similarity

    Enzyme regulationi

    Inhibited by nickel and zinc excess, and slightly activated by manganese.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi104 – 1041Zinc; catalyticBy similarity
    Active sitei107 – 1071Proton acceptor
    Metal bindingi108 – 1081Zinc; catalyticBy similarity
    Metal bindingi205 – 2051Zinc; catalyticBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. positive regulation of catalytic activity Source: GOC
    2. proteolysis Source: UniProtKB

    Keywords - Molecular functioni

    Hydrolase, Metalloprotease, Protease

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    SignaLinkiQ5JRX3.

    Protein family/group databases

    MEROPSiM16.009.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Presequence protease, mitochondrial (EC:3.4.24.-)
    Short name:
    hPreP
    Alternative name(s):
    Pitrilysin metalloproteinase 1
    Short name:
    Metalloprotease 1
    Short name:
    hMP1
    Gene namesi
    Name:PITRM1
    Synonyms:KIAA1104, MP1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:17663. PITRM1.

    Subcellular locationi

    Mitochondrion matrix 1 Publication

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi107 – 1071E → Q: Loss of function. 1 Publication
    Mutagenesisi119 – 1191C → S: Still active under oxidizing conditions. 1 Publication

    Organism-specific databases

    PharmGKBiPA134902269.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 1515Mitochondrion1 PublicationAdd
    BLAST
    Chaini16 – 10371022Presequence protease, mitochondrialPRO_0000249931Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi119 ↔ 5561 Publication
    Modified residuei759 – 7591N6-acetyllysineBy similarity
    Modified residuei770 – 7701N6-acetyllysine; alternateBy similarity
    Modified residuei770 – 7701N6-succinyllysine; alternateBy similarity
    Modified residuei849 – 8491N6-succinyllysineBy similarity
    Modified residuei884 – 8841N6-acetyllysineBy similarity
    Modified residuei946 – 9461N6-succinyllysineBy similarity

    Post-translational modificationi

    The disulfide bond may lock the enzyme in a closed conformation under oxidized conditions, suggesting that it may participate in redox regulation of the enzyme.

    Keywords - PTMi

    Acetylation, Disulfide bond

    Proteomic databases

    MaxQBiQ5JRX3.
    PaxDbiQ5JRX3.
    PRIDEiQ5JRX3.

    PTM databases

    PhosphoSiteiQ5JRX3.

    Expressioni

    Tissue specificityi

    Widely expressed. Expressed at higher level in muscle and heart compared to brain, pancreas, liver, lung and placenta.1 Publication

    Gene expression databases

    ArrayExpressiQ5JRX3.
    BgeeiQ5JRX3.
    CleanExiHS_PITRM1.
    GenevestigatoriQ5JRX3.

    Organism-specific databases

    HPAiHPA006753.
    HPA006754.

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Protein-protein interaction databases

    BioGridi115786. 10 interactions.
    IntActiQ5JRX3. 2 interactions.

    Structurei

    Secondary structure

    1
    1037
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi33 – 375
    Beta strandi49 – 579
    Helixi58 – 603
    Beta strandi62 – 698
    Turni70 – 723
    Beta strandi75 – 806
    Beta strandi84 – 9310
    Beta strandi97 – 1004
    Helixi102 – 1098
    Helixi110 – 1123
    Beta strandi114 – 1163
    Helixi122 – 1276
    Beta strandi133 – 1353
    Beta strandi141 – 15111
    Helixi153 – 16816
    Helixi174 – 1807
    Beta strandi183 – 1886
    Beta strandi196 – 1994
    Helixi201 – 2099
    Helixi213 – 22513
    Helixi230 – 2323
    Turni239 – 2413
    Helixi242 – 2443
    Helixi247 – 25711
    Helixi260 – 2623
    Beta strandi263 – 2719
    Helixi273 – 28311
    Helixi285 – 2873
    Beta strandi307 – 3137
    Beta strandi326 – 33611
    Helixi340 – 35415
    Helixi360 – 3656
    Turni366 – 3694
    Beta strandi370 – 3745
    Beta strandi379 – 3813
    Beta strandi383 – 39614
    Helixi398 – 4003
    Helixi401 – 41818
    Helixi422 – 43716
    Helixi443 – 45614
    Helixi461 – 4655
    Helixi467 – 48014
    Helixi484 – 4929
    Beta strandi499 – 5068
    Helixi510 – 52718
    Helixi531 – 54919
    Helixi562 – 5643
    Beta strandi575 – 5795
    Turni580 – 5823
    Beta strandi583 – 5897
    Beta strandi593 – 60311
    Helixi609 – 6146
    Helixi615 – 6217
    Turni622 – 6243
    Helixi632 – 64211
    Beta strandi644 – 65411
    Beta strandi661 – 67313
    Helixi674 – 6763
    Helixi677 – 68913
    Helixi696 – 71217
    Turni713 – 7175
    Helixi718 – 72710
    Turni728 – 7303
    Helixi732 – 74110
    Helixi743 – 75311
    Helixi759 – 7624
    Helixi764 – 7729
    Beta strandi773 – 7753
    Beta strandi778 – 7847
    Turni786 – 7883
    Helixi789 – 80214
    Beta strandi813 – 8153
    Beta strandi817 – 8215
    Beta strandi839 – 8446
    Beta strandi853 – 8586
    Beta strandi862 – 87110
    Helixi878 – 89316
    Helixi895 – 8995
    Turni900 – 9034
    Beta strandi906 – 9127
    Beta strandi916 – 92611
    Helixi929 – 94416
    Helixi949 – 96315
    Helixi969 – 9713
    Helixi974 – 9796
    Helixi983 – 99513
    Helixi998 – 100811
    Turni1011 – 10133
    Beta strandi1016 – 10238
    Helixi1026 – 10294
    Beta strandi1034 – 10363

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4L3TX-ray2.03A/B33-1037[»]
    4NGEX-ray2.70A/D33-1037[»]
    ProteinModelPortaliQ5JRX3.
    SMRiQ5JRX3. Positions 33-1037.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase M16 family. PreP subfamily.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG1026.
    HOVERGENiHBG082167.
    KOiK06972.
    OMAiLHKIEIQ.
    OrthoDBiEOG7KH9HZ.
    TreeFamiTF300333.

    Family and domain databases

    Gene3Di3.30.830.10. 3 hits.
    InterProiIPR011249. Metalloenz_LuxS/M16.
    IPR011237. Pept_M16_dom.
    IPR011765. Pept_M16_N.
    IPR007863. Peptidase_M16_C.
    IPR013578. Peptidase_M16C_assoc.
    [Graphical view]
    PfamiPF08367. M16C_assoc. 1 hit.
    PF00675. Peptidase_M16. 1 hit.
    PF05193. Peptidase_M16_C. 2 hits.
    [Graphical view]
    SUPFAMiSSF63411. SSF63411. 4 hits.

    Sequences (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q5JRX3-1) [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

    MWRCGGRQGL CVLRRLSGGH AHHRAWRWNS NRACERALQY KLGDKIHGFT     50
    VNQVTSVPEL FLTAVKLTHD DTGARYLHLA REDTNNLFSV QFRTTPMDST 100
    GVPHILEHTV LCGSQKYPCR DPFFKMLNRS LSTFMNAFTA SDYTLYPFST 150
    QNPKDFQNLL SVYLDATFFP CLRELDFWQE GWRLEHENPS DPQTPLVFKG 200
    VVFNEMKGAF TDNERIFSQH LQNRLLPDHT YSVVSGGDPL CIPELTWEQL 250
    KQFHATHYHP SNARFFTYGN FPLEQHLKQI HEEALSKFQK IEPSTVVPAQ 300
    TPWDKPREFQ ITCGPDSFAT DPSKQTTISV SFLLPDITDT FEAFTLSLLS 350
    SLLTSGPNSP FYKALIESGL GTDFSPDVGY NGYTREAYFS VGLQGIAEKD 400
    IETVRSLIDR TIDEVVEKGF EDDRIEALLH KIEIQMKHQS TSFGLMLTSY 450
    IASCWNHDGD PVELLKLGNQ LAKFRQCLQE NPKFLQEKVK QYFKNNQHKL 500
    TLSMRPDDKY HEKQAQVEAT KLKQKVEALS PGDRQQIYEK GLELRSQQSK 550
    PQDASCLPAL KVSDIEPTIP VTELDVVLTA GDIPVQYCAQ PTNGMVYFRA 600
    FSSLNTLPEE LRPYVPLFCS VLTKLGCGLL DYREQAQQIE LKTGGMSASP 650
    HVLPDDSHMD TYEQGVLFSS LCLDRNLPDM MQLWSEIFNN PCFEEEEHFK 700
    VLVKMTAQEL ANGIPDSGHL YASIRAGRTL TPAGDLQETF SGMDQVRLMK 750
    RIAEMTDIKP ILRKLPRIKK HLLNGDNMRC SVNATPQQMP QTEKAVEDFL 800
    RSIGRSKKER RPVRPHTVEK PVPSSSGGDA HVPHGSQVIR KLVMEPTFKP 850
    WQMKTHFLMP FPVNYVGECI RTVPYTDPDH ASLKILARLM TAKFLHTEIR 900
    EKGGAYGGGA KLSHNGIFTL YSYRDPNTIE TLQSFGKAVD WAKSGKFTQQ 950
    DIDEAKLSVF STVDAPVAPS DKGMDHFLYG LSDEMKQAHR EQLFAVSHDK 1000
    LLAVSDRYLG TGKSTHGLAI LGPENPKIAK DPSWIIQ 1037
    Length:1,037
    Mass (Da):117,413
    Last modified:May 1, 2013 - v3
    Checksum:iF488389F0E219718
    GO
    Isoform 2 (identifier: Q5JRX3-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         664-664: Q → QV

    Note: No experimental confirmation available.

    Show »
    Length:1,038
    Mass (Da):117,512
    Checksum:i8A55B3A43B434A4E
    GO
    Isoform 3 (identifier: Q5JRX3-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-53: MWRCGGRQGLCVLRRLSGGHAHHRAWRWNSNRACERALQYKLGDKIHGFTVNQ → MRNVALRRAAGPVCAEAAERR
         624-689: Missing.

    Show »
    Length:939
    Mass (Da):106,065
    Checksum:i21E09CEE32236867
    GO

    Sequence cautioni

    The sequence AAH01150.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence CAI39997.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti121 – 1211D → N in AAC67244. (PubMed:10360838)Curated
    Sequence conflicti211 – 2111T → V in CAI40001. (PubMed:15164054)Curated
    Sequence conflicti212 – 2121D → N in CAI40001. (PubMed:15164054)Curated
    Sequence conflicti373 – 3731D → E in AAC67244. (PubMed:10360838)Curated
    Sequence conflicti418 – 4203KGF → TRI in AAC67244. (PubMed:10360838)Curated
    Sequence conflicti883 – 8842LK → FE in AAH95422. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti8 – 81Q → R.1 Publication
    Corresponds to variant rs11818724 [ dbSNP | Ensembl ].
    VAR_027517
    Natural varianti145 – 1451L → V.1 Publication
    Corresponds to variant rs9423502 [ dbSNP | Ensembl ].
    VAR_027518
    Natural varianti169 – 1691F → S.1 Publication
    Corresponds to variant rs3814596 [ dbSNP | Ensembl ].
    VAR_027519
    Natural varianti328 – 3281I → V.3 Publications
    Corresponds to variant rs4242746 [ dbSNP | Ensembl ].
    VAR_027520
    Natural varianti397 – 3971A → V.3 Publications
    Corresponds to variant rs3182535 [ dbSNP | Ensembl ].
    VAR_027521
    Natural varianti516 – 5161Q → H.
    Corresponds to variant rs3765101 [ dbSNP | Ensembl ].
    VAR_027522
    Natural varianti554 – 5541A → D.
    Corresponds to variant rs12248937 [ dbSNP | Ensembl ].
    VAR_057059
    Natural varianti621 – 6211V → I.1 Publication
    Corresponds to variant rs2388556 [ dbSNP | Ensembl ].
    VAR_027523
    Natural varianti805 – 8051R → Q.
    Corresponds to variant rs34837384 [ dbSNP | Ensembl ].
    VAR_057060
    Natural varianti952 – 9521I → M.
    Corresponds to variant rs2279219 [ dbSNP | Ensembl ].
    VAR_027524
    Natural varianti963 – 9631V → I.1 Publication
    Corresponds to variant rs17849904 [ dbSNP | Ensembl ].
    VAR_027525
    Natural varianti969 – 9691P → L.
    Corresponds to variant rs2279218 [ dbSNP | Ensembl ].
    VAR_027526
    Natural varianti1037 – 10371Q → R.4 Publications
    Corresponds to variant rs6901 [ dbSNP | Ensembl ].
    VAR_027527

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 5353MWRCG…FTVNQ → MRNVALRRAAGPVCAEAAER R in isoform 3. 1 PublicationVSP_046494Add
    BLAST
    Alternative sequencei624 – 68966Missing in isoform 3. 1 PublicationVSP_046495Add
    BLAST
    Alternative sequencei664 – 6641Q → QV in isoform 2. 1 PublicationVSP_020597

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF061243 mRNA. Translation: AAC67244.1.
    AK002061 mRNA. Translation: BAG51008.1.
    AK303406 mRNA. Translation: BAG64460.1.
    AL451164 Genomic DNA. Translation: CAI40001.1.
    AL451164 Genomic DNA. Translation: CAI39997.1. Sequence problems.
    BC001150 mRNA. Translation: AAH01150.1. Different initiation.
    BC005025 mRNA. Translation: AAH05025.1.
    BC095422 mRNA. Translation: AAH95422.1.
    BC111987 mRNA. Translation: AAI11988.1.
    BC113369 mRNA. Translation: AAI13370.1.
    AB029027 mRNA. Translation: BAA83056.2.
    CCDSiCCDS55699.1. [Q5JRX3-2]
    CCDS55700.1. [Q5JRX3-3]
    CCDS59208.1. [Q5JRX3-1]
    RefSeqiNP_001229236.1. NM_001242307.1. [Q5JRX3-2]
    NP_001229238.1. NM_001242309.1. [Q5JRX3-3]
    NP_055704.2. NM_014889.3. [Q5JRX3-1]
    UniGeneiHs.528300.

    Genome annotation databases

    EnsembliENST00000224949; ENSP00000224949; ENSG00000107959. [Q5JRX3-1]
    ENST00000380989; ENSP00000370377; ENSG00000107959. [Q5JRX3-2]
    ENST00000451104; ENSP00000401201; ENSG00000107959. [Q5JRX3-3]
    GeneIDi10531.
    KEGGihsa:10531.

    Polymorphism databases

    DMDMi485956568.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF061243 mRNA. Translation: AAC67244.1 .
    AK002061 mRNA. Translation: BAG51008.1 .
    AK303406 mRNA. Translation: BAG64460.1 .
    AL451164 Genomic DNA. Translation: CAI40001.1 .
    AL451164 Genomic DNA. Translation: CAI39997.1 . Sequence problems.
    BC001150 mRNA. Translation: AAH01150.1 . Different initiation.
    BC005025 mRNA. Translation: AAH05025.1 .
    BC095422 mRNA. Translation: AAH95422.1 .
    BC111987 mRNA. Translation: AAI11988.1 .
    BC113369 mRNA. Translation: AAI13370.1 .
    AB029027 mRNA. Translation: BAA83056.2 .
    CCDSi CCDS55699.1. [Q5JRX3-2 ]
    CCDS55700.1. [Q5JRX3-3 ]
    CCDS59208.1. [Q5JRX3-1 ]
    RefSeqi NP_001229236.1. NM_001242307.1. [Q5JRX3-2 ]
    NP_001229238.1. NM_001242309.1. [Q5JRX3-3 ]
    NP_055704.2. NM_014889.3. [Q5JRX3-1 ]
    UniGenei Hs.528300.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4L3T X-ray 2.03 A/B 33-1037 [» ]
    4NGE X-ray 2.70 A/D 33-1037 [» ]
    ProteinModelPortali Q5JRX3.
    SMRi Q5JRX3. Positions 33-1037.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115786. 10 interactions.
    IntActi Q5JRX3. 2 interactions.

    Protein family/group databases

    MEROPSi M16.009.

    PTM databases

    PhosphoSitei Q5JRX3.

    Polymorphism databases

    DMDMi 485956568.

    Proteomic databases

    MaxQBi Q5JRX3.
    PaxDbi Q5JRX3.
    PRIDEi Q5JRX3.

    Protocols and materials databases

    DNASUi 10531.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000224949 ; ENSP00000224949 ; ENSG00000107959 . [Q5JRX3-1 ]
    ENST00000380989 ; ENSP00000370377 ; ENSG00000107959 . [Q5JRX3-2 ]
    ENST00000451104 ; ENSP00000401201 ; ENSG00000107959 . [Q5JRX3-3 ]
    GeneIDi 10531.
    KEGGi hsa:10531.

    Organism-specific databases

    CTDi 10531.
    GeneCardsi GC10M003179.
    H-InvDB HIX0008597.
    HGNCi HGNC:17663. PITRM1.
    HPAi HPA006753.
    HPA006754.
    neXtProti NX_Q5JRX3.
    PharmGKBi PA134902269.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1026.
    HOVERGENi HBG082167.
    KOi K06972.
    OMAi LHKIEIQ.
    OrthoDBi EOG7KH9HZ.
    TreeFami TF300333.

    Enzyme and pathway databases

    SignaLinki Q5JRX3.

    Miscellaneous databases

    ChiTaRSi PITRM1. human.
    GeneWikii PITRM1.
    GenomeRNAii 10531.
    NextBioi 39957.
    PROi Q5JRX3.

    Gene expression databases

    ArrayExpressi Q5JRX3.
    Bgeei Q5JRX3.
    CleanExi HS_PITRM1.
    Genevestigatori Q5JRX3.

    Family and domain databases

    Gene3Di 3.30.830.10. 3 hits.
    InterProi IPR011249. Metalloenz_LuxS/M16.
    IPR011237. Pept_M16_dom.
    IPR011765. Pept_M16_N.
    IPR007863. Peptidase_M16_C.
    IPR013578. Peptidase_M16C_assoc.
    [Graphical view ]
    Pfami PF08367. M16C_assoc. 1 hit.
    PF00675. Peptidase_M16. 1 hit.
    PF05193. Peptidase_M16_C. 2 hits.
    [Graphical view ]
    SUPFAMi SSF63411. SSF63411. 4 hits.
    ProtoNeti Search...

    Publicationsi

    1. "Cloning, expression, and characterization of human metalloprotease 1: a novel member of the pitrilysin family of metalloendoproteases."
      Mzhavia N., Berman Y.L., Qian Y., Yan L., Devi L.A.
      DNA Cell Biol. 18:369-380(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, VARIANTS SER-169; VAL-328; VAL-397; ILE-621 AND ARG-1037.
    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] (ISOFORMS 1 AND 3), VARIANTS VAL-328; VAL-397 AND ARG-1037.
      Tissue: Placenta and Thymus.
    3. "The DNA sequence and comparative analysis of human chromosome 10."
      Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
      , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
      Nature 429:375-381(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] (ISOFORM 1), VARIANTS ARG-8; VAL-145; VAL-328; VAL-397; ILE-963 AND ARG-1037.
      Tissue: Brain, Lung and Testis.
    5. "Prediction of the coding sequences of unidentified human genes. XIV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
      Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 6:197-205(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 402-1037 (ISOFORM 1), VARIANT ARG-1037.
      Tissue: Brain.
    6. "Degradation of the amyloid beta-protein by the novel mitochondrial peptidasome, PreP."
      Falkevall A., Alikhani N., Bhushan S., Pavlov P.F., Busch K., Johnson K.A., Eneqvist T., Tjernberg L., Ankarcrona M., Glaser E.
      J. Biol. Chem. 281:29096-29104(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, DISULFIDE BOND, MUTAGENESIS OF GLU-107 AND CYS-119.
    7. "Mammalian pitrilysin: substrate specificity and mitochondrial targeting."
      Chow K.M., Gakh O., Payne I.C., Juliano M.A., Juliano L., Isaya G., Hersh L.B.
      Biochemistry 48:2868-2877(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: TRANSIT PEPTIDE CLEAVAGE SITE, ENZYME REGULATION, SUBSTRATE SPECIFICITY.
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiPREP_HUMAN
    AccessioniPrimary (citable) accession number: Q5JRX3
    Secondary accession number(s): B3KMJ6
    , B4E0J8, C9JSL2, E7ES23, O95204, Q2M2G6, Q4VBR1, Q5JRW7, Q7L5Z7, Q9BSI6, Q9BVJ5, Q9UPP8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 19, 2006
    Last sequence update: May 1, 2013
    Last modified: October 1, 2014
    This is version 97 of the entry and version 3 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 10
      Human chromosome 10: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    5. Peptidase families
      Classification of peptidase families and list of entries
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3