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Q5JRX3

- PREP_HUMAN

UniProt

Q5JRX3 - PREP_HUMAN

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Protein

Presequence protease, mitochondrial

Gene

PITRM1

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

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

Zn2+By similarityNote: 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
Complete GO annotation...

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
Complete GO annotation...

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

BgeeiQ5JRX3.
CleanExiHS_PITRM1.
ExpressionAtlasiQ5JRX3. baseline and differential.
GenevestigatoriQ5JRX3.

Organism-specific databases

HPAiHPA006753.
HPA006754.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

BioGridi115786. 13 interactions.
DIPiDIP-52900N.
IntActiQ5JRX3. 2 interactions.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00390000018381.
HOVERGENiHBG082167.
InParanoidiQ5JRX3.
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

        10         20         30         40         50
MWRCGGRQGL CVLRRLSGGH AHHRAWRWNS NRACERALQY KLGDKIHGFT
60 70 80 90 100
VNQVTSVPEL FLTAVKLTHD DTGARYLHLA REDTNNLFSV QFRTTPMDST
110 120 130 140 150
GVPHILEHTV LCGSQKYPCR DPFFKMLNRS LSTFMNAFTA SDYTLYPFST
160 170 180 190 200
QNPKDFQNLL SVYLDATFFP CLRELDFWQE GWRLEHENPS DPQTPLVFKG
210 220 230 240 250
VVFNEMKGAF TDNERIFSQH LQNRLLPDHT YSVVSGGDPL CIPELTWEQL
260 270 280 290 300
KQFHATHYHP SNARFFTYGN FPLEQHLKQI HEEALSKFQK IEPSTVVPAQ
310 320 330 340 350
TPWDKPREFQ ITCGPDSFAT DPSKQTTISV SFLLPDITDT FEAFTLSLLS
360 370 380 390 400
SLLTSGPNSP FYKALIESGL GTDFSPDVGY NGYTREAYFS VGLQGIAEKD
410 420 430 440 450
IETVRSLIDR TIDEVVEKGF EDDRIEALLH KIEIQMKHQS TSFGLMLTSY
460 470 480 490 500
IASCWNHDGD PVELLKLGNQ LAKFRQCLQE NPKFLQEKVK QYFKNNQHKL
510 520 530 540 550
TLSMRPDDKY HEKQAQVEAT KLKQKVEALS PGDRQQIYEK GLELRSQQSK
560 570 580 590 600
PQDASCLPAL KVSDIEPTIP VTELDVVLTA GDIPVQYCAQ PTNGMVYFRA
610 620 630 640 650
FSSLNTLPEE LRPYVPLFCS VLTKLGCGLL DYREQAQQIE LKTGGMSASP
660 670 680 690 700
HVLPDDSHMD TYEQGVLFSS LCLDRNLPDM MQLWSEIFNN PCFEEEEHFK
710 720 730 740 750
VLVKMTAQEL ANGIPDSGHL YASIRAGRTL TPAGDLQETF SGMDQVRLMK
760 770 780 790 800
RIAEMTDIKP ILRKLPRIKK HLLNGDNMRC SVNATPQQMP QTEKAVEDFL
810 820 830 840 850
RSIGRSKKER RPVRPHTVEK PVPSSSGGDA HVPHGSQVIR KLVMEPTFKP
860 870 880 890 900
WQMKTHFLMP FPVNYVGECI RTVPYTDPDH ASLKILARLM TAKFLHTEIR
910 920 930 940 950
EKGGAYGGGA KLSHNGIFTL YSYRDPNTIE TLQSFGKAVD WAKSGKFTQQ
960 970 980 990 1000
DIDEAKLSVF STVDAPVAPS DKGMDHFLYG LSDEMKQAHR EQLFAVSHDK
1010 1020 1030
LLAVSDRYLG TGKSTHGLAI LGPENPKIAK DPSWIIQ
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.Curated
The sequence CAI39997.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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. 13 interactions.
DIPi DIP-52900N.
IntActi Q5JRX3. 2 interactions.

Chemistry

ChEMBLi CHEMBL3124731.

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.
GeneTreei ENSGT00390000018381.
HOVERGENi HBG082167.
InParanoidi Q5JRX3.
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

Bgeei Q5JRX3.
CleanExi HS_PITRM1.
ExpressionAtlasi Q5JRX3. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 99 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