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Protein

Presequence protease, mitochondrial

Gene

PITRM1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Metal bindingi104Zinc; catalyticBy similarity1
Active sitei107Proton acceptor1
Metal bindingi108Zinc; catalyticBy similarity1
Metal bindingi205Zinc; catalyticBy similarity1

GO - Molecular functioni

  • enzyme activator activity Source: ProtInc
  • metalloendopeptidase activity Source: UniProtKB
  • zinc ion binding Source: GO_Central

GO - Biological processi

  • protein processing Source: GO_Central
  • 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
Proteomesi
  • UP000005640 Componenti: Chromosome 10

Organism-specific databases

HGNCiHGNC:17663. PITRM1.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial matrix Source: UniProtKB
  • mitochondrion Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi107E → Q: Loss of function. 1 Publication1
Mutagenesisi119C → S: Still active under oxidizing conditions. 1 Publication1

Organism-specific databases

DisGeNETi10531.
OpenTargetsiENSG00000107959.
PharmGKBiPA134902269.

Chemistry databases

ChEMBLiCHEMBL3124731.

Polymorphism and mutation databases

BioMutaiPITRM1.
DMDMi485956568.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 15Mitochondrion1 PublicationAdd BLAST15
ChainiPRO_000024993116 – 1037Presequence protease, mitochondrialAdd BLAST1022

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi119 ↔ 5561 Publication
Modified residuei759N6-acetyllysineBy similarity1
Modified residuei770N6-acetyllysine; alternateBy similarity1
Modified residuei770N6-succinyllysine; alternateBy similarity1
Modified residuei849N6-succinyllysineBy similarity1
Modified residuei884N6-acetyllysineBy similarity1
Modified residuei946N6-succinyllysineBy similarity1

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

EPDiQ5JRX3.
MaxQBiQ5JRX3.
PaxDbiQ5JRX3.
PeptideAtlasiQ5JRX3.
PRIDEiQ5JRX3.

PTM databases

iPTMnetiQ5JRX3.
PhosphoSitePlusiQ5JRX3.
SwissPalmiQ5JRX3.

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

BgeeiENSG00000107959.
CleanExiHS_PITRM1.
ExpressionAtlasiQ5JRX3. baseline and differential.
GenevisibleiQ5JRX3. HS.

Organism-specific databases

HPAiHPA006753.
HPA006754.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

BioGridi115786. 35 interactors.
DIPiDIP-52900N.
IntActiQ5JRX3. 3 interactors.
STRINGi9606.ENSP00000370377.

Chemistry databases

BindingDBiQ5JRX3.

Structurei

Secondary structure

11037
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi33 – 37Combined sources5
Beta strandi49 – 57Combined sources9
Helixi58 – 60Combined sources3
Beta strandi62 – 69Combined sources8
Turni70 – 72Combined sources3
Beta strandi75 – 80Combined sources6
Beta strandi84 – 93Combined sources10
Beta strandi97 – 100Combined sources4
Helixi102 – 109Combined sources8
Helixi110 – 112Combined sources3
Beta strandi114 – 116Combined sources3
Helixi122 – 127Combined sources6
Beta strandi133 – 135Combined sources3
Beta strandi141 – 151Combined sources11
Helixi153 – 168Combined sources16
Helixi174 – 180Combined sources7
Beta strandi183 – 188Combined sources6
Beta strandi192 – 194Combined sources3
Beta strandi196 – 199Combined sources4
Helixi201 – 209Combined sources9
Helixi213 – 225Combined sources13
Helixi230 – 232Combined sources3
Turni239 – 241Combined sources3
Helixi242 – 244Combined sources3
Helixi247 – 257Combined sources11
Helixi260 – 262Combined sources3
Beta strandi263 – 271Combined sources9
Helixi273 – 283Combined sources11
Helixi285 – 287Combined sources3
Beta strandi307 – 313Combined sources7
Helixi322 – 324Combined sources3
Beta strandi326 – 336Combined sources11
Helixi340 – 354Combined sources15
Helixi360 – 365Combined sources6
Turni366 – 369Combined sources4
Beta strandi370 – 374Combined sources5
Beta strandi379 – 381Combined sources3
Beta strandi383 – 396Combined sources14
Helixi398 – 400Combined sources3
Helixi401 – 418Combined sources18
Helixi422 – 437Combined sources16
Helixi443 – 456Combined sources14
Helixi461 – 465Combined sources5
Helixi467 – 480Combined sources14
Helixi484 – 492Combined sources9
Beta strandi499 – 506Combined sources8
Helixi510 – 527Combined sources18
Helixi531 – 549Combined sources19
Helixi562 – 564Combined sources3
Beta strandi575 – 579Combined sources5
Turni580 – 582Combined sources3
Beta strandi583 – 589Combined sources7
Beta strandi593 – 603Combined sources11
Helixi609 – 614Combined sources6
Helixi615 – 621Combined sources7
Turni622 – 624Combined sources3
Helixi632 – 642Combined sources11
Beta strandi644 – 654Combined sources11
Beta strandi661 – 673Combined sources13
Helixi674 – 676Combined sources3
Helixi677 – 689Combined sources13
Helixi696 – 712Combined sources17
Turni713 – 717Combined sources5
Helixi718 – 727Combined sources10
Turni728 – 730Combined sources3
Helixi732 – 741Combined sources10
Helixi743 – 753Combined sources11
Helixi759 – 762Combined sources4
Helixi764 – 772Combined sources9
Beta strandi773 – 775Combined sources3
Beta strandi778 – 784Combined sources7
Turni786 – 788Combined sources3
Helixi789 – 802Combined sources14
Beta strandi813 – 815Combined sources3
Beta strandi817 – 821Combined sources5
Beta strandi839 – 844Combined sources6
Beta strandi853 – 858Combined sources6
Beta strandi862 – 871Combined sources10
Helixi878 – 893Combined sources16
Helixi895 – 899Combined sources5
Turni900 – 903Combined sources4
Beta strandi906 – 912Combined sources7
Beta strandi916 – 926Combined sources11
Helixi929 – 944Combined sources16
Helixi949 – 963Combined sources15
Helixi969 – 971Combined sources3
Helixi974 – 979Combined sources6
Helixi983 – 995Combined sources13
Helixi998 – 1008Combined sources11
Turni1011 – 1013Combined sources3
Beta strandi1016 – 1023Combined sources8
Helixi1026 – 1029Combined sources4
Beta strandi1034 – 1036Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4L3TX-ray2.03A/B33-1037[»]
4NGEX-ray2.70A/D33-1037[»]
4RPUX-ray2.27A/B33-1037[»]
ProteinModelPortaliQ5JRX3.
SMRiQ5JRX3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M16 family. PreP subfamily.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG2019. Eukaryota.
COG1026. LUCA.
GeneTreeiENSGT00390000018381.
HOGENOMiHOG000008829.
HOVERGENiHBG082167.
InParanoidiQ5JRX3.
KOiK06972.
OMAiPVRPHVI.
OrthoDBiEOG091G0108.
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]
SMARTiSM01264. M16C_associated. 1 hit.
[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. AlignAdd to basket

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti121D → N in AAC67244 (PubMed:10360838).Curated1
Sequence conflicti211T → V in CAI40001 (PubMed:15164054).Curated1
Sequence conflicti212D → N in CAI40001 (PubMed:15164054).Curated1
Sequence conflicti373D → E in AAC67244 (PubMed:10360838).Curated1
Sequence conflicti418 – 420KGF → TRI in AAC67244 (PubMed:10360838).Curated3
Sequence conflicti883 – 884LK → FE in AAH95422 (PubMed:15489334).Curated2

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0275178Q → R.1 PublicationCorresponds to variant rs11818724dbSNPEnsembl.1
Natural variantiVAR_027518145L → V.1 PublicationCorresponds to variant rs9423502dbSNPEnsembl.1
Natural variantiVAR_027519169F → S.1 PublicationCorresponds to variant rs3814596dbSNPEnsembl.1
Natural variantiVAR_027520328I → V.3 PublicationsCorresponds to variant rs4242746dbSNPEnsembl.1
Natural variantiVAR_027521397A → V.3 PublicationsCorresponds to variant rs3182535dbSNPEnsembl.1
Natural variantiVAR_027522516Q → H.Corresponds to variant rs3765101dbSNPEnsembl.1
Natural variantiVAR_057059554A → D.Corresponds to variant rs12248937dbSNPEnsembl.1
Natural variantiVAR_027523621V → I.1 PublicationCorresponds to variant rs2388556dbSNPEnsembl.1
Natural variantiVAR_057060805R → Q.Corresponds to variant rs34837384dbSNPEnsembl.1
Natural variantiVAR_027524952I → M.Corresponds to variant rs2279219dbSNPEnsembl.1
Natural variantiVAR_027525963V → I.1 PublicationCorresponds to variant rs17849904dbSNPEnsembl.1
Natural variantiVAR_027526969P → L.Corresponds to variant rs2279218dbSNPEnsembl.1
Natural variantiVAR_0275271037Q → R.Combined sources4 PublicationsCorresponds to variant rs6901dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0464941 – 53MWRCG…FTVNQ → MRNVALRRAAGPVCAEAAER R in isoform 3. 1 PublicationAdd BLAST53
Alternative sequenceiVSP_046495624 – 689Missing in isoform 3. 1 PublicationAdd BLAST66
Alternative sequenceiVSP_020597664Q → QV in isoform 2. 1 Publication1

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.
UCSCiuc001igt.3. human. [Q5JRX3-1]

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.
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4L3TX-ray2.03A/B33-1037[»]
4NGEX-ray2.70A/D33-1037[»]
4RPUX-ray2.27A/B33-1037[»]
ProteinModelPortaliQ5JRX3.
SMRiQ5JRX3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115786. 35 interactors.
DIPiDIP-52900N.
IntActiQ5JRX3. 3 interactors.
STRINGi9606.ENSP00000370377.

Chemistry databases

BindingDBiQ5JRX3.
ChEMBLiCHEMBL3124731.

Protein family/group databases

MEROPSiM16.009.

PTM databases

iPTMnetiQ5JRX3.
PhosphoSitePlusiQ5JRX3.
SwissPalmiQ5JRX3.

Polymorphism and mutation databases

BioMutaiPITRM1.
DMDMi485956568.

Proteomic databases

EPDiQ5JRX3.
MaxQBiQ5JRX3.
PaxDbiQ5JRX3.
PeptideAtlasiQ5JRX3.
PRIDEiQ5JRX3.

Protocols and materials databases

DNASUi10531.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000224949; ENSP00000224949; ENSG00000107959. [Q5JRX3-1]
ENST00000380989; ENSP00000370377; ENSG00000107959. [Q5JRX3-2]
ENST00000451104; ENSP00000401201; ENSG00000107959. [Q5JRX3-3]
GeneIDi10531.
KEGGihsa:10531.
UCSCiuc001igt.3. human. [Q5JRX3-1]

Organism-specific databases

CTDi10531.
DisGeNETi10531.
GeneCardsiPITRM1.
H-InvDBHIX0008597.
HGNCiHGNC:17663. PITRM1.
HPAiHPA006753.
HPA006754.
neXtProtiNX_Q5JRX3.
OpenTargetsiENSG00000107959.
PharmGKBiPA134902269.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2019. Eukaryota.
COG1026. LUCA.
GeneTreeiENSGT00390000018381.
HOGENOMiHOG000008829.
HOVERGENiHBG082167.
InParanoidiQ5JRX3.
KOiK06972.
OMAiPVRPHVI.
OrthoDBiEOG091G0108.
TreeFamiTF300333.

Enzyme and pathway databases

SignaLinkiQ5JRX3.

Miscellaneous databases

ChiTaRSiPITRM1. human.
GeneWikiiPITRM1.
GenomeRNAii10531.
PROiQ5JRX3.

Gene expression databases

BgeeiENSG00000107959.
CleanExiHS_PITRM1.
ExpressionAtlasiQ5JRX3. baseline and differential.
GenevisibleiQ5JRX3. HS.

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]
SMARTiSM01264. M16C_associated. 1 hit.
[Graphical view]
SUPFAMiSSF63411. SSF63411. 4 hits.
ProtoNetiSearch...

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 2, 2016
This is version 117 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

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 one 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.