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O43464

- HTRA2_HUMAN

UniProt

O43464 - HTRA2_HUMAN

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Protein

Serine protease HTRA2, mitochondrial

Gene

HTRA2

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

Functioni

Serine protease that shows proteolytic activity against a non-specific substrate beta-casein. Promotes or induces cell death either by direct binding to and inhibition of BIRC proteins (also called inhibitor of apoptosis proteins, IAPs), leading to an increase in caspase activity, or by a BIRC inhibition-independent, caspase-independent and serine protease activity-dependent mechanism. Cleaves THAP5 and promotes its degradation during apoptosis. Isoform 2 seems to be proteolytically inactive.2 Publications

Catalytic activityi

Cleavage of non-polar aliphatic amino acids at the P1 position, with a preference for Val, Ile and Met. At the P2 and P3 positions, Arg is selected most strongly with a secondary preference for other hydrophilic residues.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei198 – 1981Charge relay system
Active sitei228 – 2281Charge relay system
Active sitei306 – 3061Charge relay system

GO - Molecular functioni

  1. peptidase activity Source: UniProtKB
  2. serine-type endopeptidase activity Source: UniProtKB
  3. serine-type peptidase activity Source: UniProtKB
  4. unfolded protein binding Source: UniProtKB

GO - Biological processi

  1. adult walking behavior Source: Ensembl
  2. cellular protein catabolic process Source: ParkinsonsUK-UCL
  3. cellular response to growth factor stimulus Source: UniProtKB
  4. cellular response to heat Source: UniProtKB
  5. cellular response to interferon-beta Source: ParkinsonsUK-UCL
  6. cellular response to oxidative stress Source: ParkinsonsUK-UCL
  7. cellular response to retinoic acid Source: ParkinsonsUK-UCL
  8. ceramide metabolic process Source: Ensembl
  9. execution phase of apoptosis Source: UniProtKB
  10. forebrain development Source: Ensembl
  11. intrinsic apoptotic signaling pathway in response to DNA damage Source: ParkinsonsUK-UCL
  12. mitochondrion organization Source: Ensembl
  13. negative regulation of cell cycle Source: UniProtKB
  14. negative regulation of neuron death Source: ParkinsonsUK-UCL
  15. negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway Source: ParkinsonsUK-UCL
  16. neuron development Source: Ensembl
  17. pentacyclic triterpenoid metabolic process Source: Ensembl
  18. positive regulation of apoptotic process Source: UniProtKB
  19. positive regulation of cell death Source: UniProtKB
  20. positive regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
  21. positive regulation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway Source: ParkinsonsUK-UCL
  22. positive regulation of extrinsic apoptotic signaling pathway in absence of ligand Source: UniProtKB
  23. protein autoprocessing Source: ParkinsonsUK-UCL
  24. proteolysis Source: UniProtKB
  25. regulation of mitochondrion degradation Source: ParkinsonsUK-UCL
  26. regulation of multicellular organism growth Source: Ensembl
  27. response to herbicide Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Biological processi

Apoptosis

Enzyme and pathway databases

BRENDAi3.4.21.108. 2681.

Protein family/group databases

MEROPSiS01.278.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine protease HTRA2, mitochondrial (EC:3.4.21.108)
Alternative name(s):
High temperature requirement protein A2
Short name:
HtrA2
Omi stress-regulated endoprotease
Serine protease 25
Serine proteinase OMI
Gene namesi
Name:HTRA2
Synonyms:OMI, PRSS25
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:14348. HTRA2.

Subcellular locationi

Mitochondrion intermembrane space. Mitochondrion membrane Curated; Single-pass membrane protein Curated
Note: Predominantly present in the intermembrane space. Released into the cytosol following apoptotic stimuli, such as UV treatment, and stimulation of mitochondria with caspase-8 truncated BID/tBID.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei105 – 12521HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. CD40 receptor complex Source: BHF-UCL
  2. chromatin Source: ParkinsonsUK-UCL
  3. cytoplasmic side of plasma membrane Source: BHF-UCL
  4. cytoskeleton Source: ParkinsonsUK-UCL
  5. cytosol Source: ParkinsonsUK-UCL
  6. endoplasmic reticulum Source: UniProtKB
  7. endoplasmic reticulum membrane Source: UniProtKB
  8. membrane Source: ParkinsonsUK-UCL
  9. mitochondrial intermembrane space Source: MGI
  10. mitochondrion Source: UniProtKB
  11. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion

Pathology & Biotechi

Involvement in diseasei

Parkinson disease 13 (PARK13) [MIM:610297]: A complex neurodegenerative disorder characterized by bradykinesia, resting tremor, muscular rigidity and postural instability, as well as by a clinically significant response to treatment with levodopa. The pathology involves the loss of dopaminergic neurons in the substantia nigra and the presence of Lewy bodies (intraneuronal accumulations of aggregated proteins), in surviving neurons in various areas of the brain.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti399 – 3991G → S in PARK13; reduced protease activity. 1 Publication
Corresponds to variant rs72470545 [ dbSNP | Ensembl ].
VAR_027350

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi134 – 1341A → M: Loss of interaction with XIAP. Loss of inhibition of XIAP activity. 1 Publication
Mutagenesisi306 – 3061S → A: Loss of protease activity. 1 Publication

Keywords - Diseasei

Disease mutation, Neurodegeneration, Parkinson disease, Parkinsonism

Organism-specific databases

MIMi168600. phenotype.
610297. phenotype.
Orphaneti2828. Young adult-onset Parkinsonism.
PharmGKBiPA33836.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3131MitochondrionAdd
BLAST
Propeptidei32 – 1331021 PublicationPRO_0000026945Add
BLAST
Chaini134 – 458325Serine protease HTRA2, mitochondrialPRO_0000026946Add
BLAST

Post-translational modificationi

Autoproteolytically activated.

Keywords - PTMi

Autocatalytic cleavage, Zymogen

Proteomic databases

MaxQBiO43464.
PaxDbiO43464.
PRIDEiO43464.

2D gel databases

OGPiO43464.

PTM databases

PhosphoSiteiO43464.

Miscellaneous databases

PMAP-CutDBO43464.

Expressioni

Tissue specificityi

Isoform 1 is ubiquitous. Isoform 2 is expressed predominantly in the kidney, colon and thyroid.

Gene expression databases

BgeeiO43464.
CleanExiHS_HTRA2.
GenevestigatoriO43464.

Organism-specific databases

HPAiCAB004004.
HPA027366.

Interactioni

Subunit structurei

Homotrimer. Interacts with MXI2. Interacts with THAP5 under apoptotic conditions. The mature protein, but not the precursor, binds to BIRC2/c-IAP1, BIRC3/c-IAP2 and XIAP/BIRC4. Interacts with BIRC6/bruce.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BIRC7Q96CA52EBI-517086,EBI-517623
CSN2P026665EBI-517086,EBI-5260183From a different organism.
NDUFA13Q9P0J06EBI-517086,EBI-372742
Ripk1Q608552EBI-517086,EBI-529119From a different organism.
XIAPP9817018EBI-517086,EBI-517127

Protein-protein interaction databases

BioGridi118165. 50 interactions.
IntActiO43464. 37 interactions.
MINTiMINT-216075.
STRINGi9606.ENSP00000258080.

Structurei

Secondary structure

1
458
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi143 – 1464Combined sources
Helixi149 – 1579Combined sources
Helixi158 – 1603Combined sources
Beta strandi161 – 17010Combined sources
Turni171 – 1744Combined sources
Beta strandi175 – 18814Combined sources
Turni189 – 1913Combined sources
Beta strandi192 – 1954Combined sources
Helixi197 – 2004Combined sources
Beta strandi204 – 2096Combined sources
Beta strandi215 – 22410Combined sources
Turni225 – 2284Combined sources
Beta strandi229 – 2335Combined sources
Helixi248 – 2503Combined sources
Beta strandi256 – 2594Combined sources
Beta strandi265 – 2684Combined sources
Beta strandi271 – 2755Combined sources
Beta strandi295 – 2995Combined sources
Turni303 – 3075Combined sources
Beta strandi308 – 3125Combined sources
Beta strandi317 – 32610Combined sources
Beta strandi329 – 3346Combined sources
Helixi335 – 3417Combined sources
Beta strandi364 – 3685Combined sources
Helixi371 – 3777Combined sources
Beta strandi391 – 3966Combined sources
Helixi401 – 4055Combined sources
Beta strandi412 – 4165Combined sources
Helixi424 – 4318Combined sources
Beta strandi435 – 4439Combined sources
Beta strandi446 – 4527Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LCYX-ray2.00A134-458[»]
2PZDX-ray2.75A/B359-458[»]
DisProtiDP00315.
ProteinModelPortaliO43464.
SMRiO43464. Positions 139-458.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO43464.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini364 – 44582PDZPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni166 – 342177Serine proteaseAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi134 – 1374IAP-binding motif

Domaini

The mature N-terminus is involved in the interaction with XIAP.
The PDZ domain mediates interaction with MXI2.

Sequence similaritiesi

Belongs to the peptidase S1C family.Curated
Contains 1 PDZ (DHR) domain.PROSITE-ProRule annotation

Keywords - Domaini

Transit peptide, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0265.
GeneTreeiENSGT00510000046315.
HOGENOMiHOG000223641.
HOVERGENiHBG052044.
InParanoidiO43464.
KOiK08669.
OMAiFKEECTE.
OrthoDBiEOG7V1FR7.
PhylomeDBiO43464.
TreeFamiTF323480.

Family and domain databases

Gene3Di2.30.42.10. 1 hit.
InterProiIPR001478. PDZ.
IPR001254. Peptidase_S1.
IPR001940. Peptidase_S1C.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamiPF13180. PDZ_2. 1 hit.
[Graphical view]
PRINTSiPR00834. PROTEASES2C.
SMARTiSM00228. PDZ. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50156. SSF50156. 1 hit.
SSF50494. SSF50494. 1 hit.
PROSITEiPS50106. PDZ. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

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

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O43464-1) [UniParc]FASTAAdd to Basket

Also known as: 13B

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
MAAPRAGRGA GWSLRAWRAL GGIRWGRRPR LTPDLRALLT SGTSDPRARV
60 70 80 90 100
TYGTPSLWAR LSVGVTEPRA CLTSGTPGPR AQLTAVTPDT RTREASENSG
110 120 130 140 150
TRSRAWLAVA LGAGGAVLLL LWGGGRGPPA VLAAVPSPPP ASPRSQYNFI
160 170 180 190 200
ADVVEKTAPA VVYIEILDRH PFLGREVPIS NGSGFVVAAD GLIVTNAHVV
210 220 230 240 250
ADRRRVRVRL LSGDTYEAVV TAVDPVADIA TLRIQTKEPL PTLPLGRSAD
260 270 280 290 300
VRQGEFVVAM GSPFALQNTI TSGIVSSAQR PARDLGLPQT NVEYIQTDAA
310 320 330 340 350
IDFGNSGGPL VNLDGEVIGV NTMKVTAGIS FAIPSDRLRE FLHRGEKKNS
360 370 380 390 400
SSGISGSQRR YIGVMMLTLS PSILAELQLR EPSFPDVQHG VLIHKVILGS
410 420 430 440 450
PAHRAGLRPG DVILAIGEQM VQNAEDVYEA VRTQSQLAVQ IRRGRETLTL

YVTPEVTE
Length:458
Mass (Da):48,841
Last modified:May 1, 2000 - v2
Checksum:iCEA955A7D0DD8C0D
GO
Isoform 2 (identifier: O43464-2) [UniParc]FASTAAdd to Basket

Also known as: D-Omi

The sequence of this isoform differs from the canonical sequence as follows:
     238-302: Missing.
     372-403: Missing.

Show »
Length:361
Mass (Da):38,493
Checksum:iBD0824D4308140D7
GO
Isoform 3 (identifier: O43464-3) [UniParc]FASTAAdd to Basket

Also known as: p7

The sequence of this isoform differs from the canonical sequence as follows:
     313-313: L → LARELGAVSLQ
     372-403: Missing.

Show »
Length:436
Mass (Da):46,382
Checksum:iB48266A8EB7E4EE8
GO
Isoform 4 (identifier: O43464-4) [UniParc]FASTAAdd to Basket

Also known as: p4

The sequence of this isoform differs from the canonical sequence as follows:
     314-458: DGEVIGVNTM...TLYVTPEVTE → VSETSFLPRI...FGCPHPLLFV

Show »
Length:377
Mass (Da):39,914
Checksum:i14D0982E08A58FB2
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti72 – 721L → P.1 Publication
Corresponds to variant rs150047108 [ dbSNP | Ensembl ].
VAR_046134
Natural varianti141 – 1411A → S Polymorphism; associated with a 2.15-fold increased risk of PD; reduced protease activity. 2 Publications
Corresponds to variant rs72470544 [ dbSNP | Ensembl ].
VAR_027349
Natural varianti399 – 3991G → S in PARK13; reduced protease activity. 1 Publication
Corresponds to variant rs72470545 [ dbSNP | Ensembl ].
VAR_027350
Natural varianti404 – 4041R → W Could be associated with an increased risk of developing PD. 1 Publication
VAR_046135

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei238 – 30265Missing in isoform 2. 1 PublicationVSP_005359Add
BLAST
Alternative sequencei313 – 3131L → LARELGAVSLQ in isoform 3. 1 PublicationVSP_005360
Alternative sequencei314 – 458145DGEVI…PEVTE → VSETSFLPRIPAPGQCGKGR FPLIQGCLVKFLSSSLLAIS QYPTRSPQHLLVLLFGCPHP LLFV in isoform 4. 1 PublicationVSP_005362Add
BLAST
Alternative sequencei372 – 40332Missing in isoform 2 and isoform 3. 2 PublicationsVSP_005361Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF020760 mRNA. Translation: AAB94569.2.
AF141305 mRNA. Translation: AAF66596.1.
AF141306 mRNA. Translation: AAF66597.1.
AF141307 mRNA. Translation: AAF66598.1.
AF184911 mRNA. Translation: AAG13126.1.
AC006544 Genomic DNA. No translation available.
BC000096 mRNA. Translation: AAH00096.1.
CCDSiCCDS1951.1. [O43464-1]
CCDS1952.1. [O43464-2]
RefSeqiNP_037379.1. NM_013247.4. [O43464-1]
NP_659540.1. NM_145074.2. [O43464-2]
UniGeneiHs.469045.
Hs.744841.

Genome annotation databases

EnsembliENST00000258080; ENSP00000258080; ENSG00000115317. [O43464-1]
ENST00000352222; ENSP00000312893; ENSG00000115317. [O43464-2]
ENST00000437202; ENSP00000399166; ENSG00000115317.
GeneIDi27429.
KEGGihsa:27429.
UCSCiuc002smi.1. human. [O43464-1]
uc002smj.1. human. [O43464-2]
uc002smk.1. human. [O43464-3]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF020760 mRNA. Translation: AAB94569.2 .
AF141305 mRNA. Translation: AAF66596.1 .
AF141306 mRNA. Translation: AAF66597.1 .
AF141307 mRNA. Translation: AAF66598.1 .
AF184911 mRNA. Translation: AAG13126.1 .
AC006544 Genomic DNA. No translation available.
BC000096 mRNA. Translation: AAH00096.1 .
CCDSi CCDS1951.1. [O43464-1 ]
CCDS1952.1. [O43464-2 ]
RefSeqi NP_037379.1. NM_013247.4. [O43464-1 ]
NP_659540.1. NM_145074.2. [O43464-2 ]
UniGenei Hs.469045.
Hs.744841.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1LCY X-ray 2.00 A 134-458 [» ]
2PZD X-ray 2.75 A/B 359-458 [» ]
DisProti DP00315.
ProteinModelPortali O43464.
SMRi O43464. Positions 139-458.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 118165. 50 interactions.
IntActi O43464. 37 interactions.
MINTi MINT-216075.
STRINGi 9606.ENSP00000258080.

Protein family/group databases

MEROPSi S01.278.

PTM databases

PhosphoSitei O43464.

2D gel databases

OGPi O43464.

Proteomic databases

MaxQBi O43464.
PaxDbi O43464.
PRIDEi O43464.

Protocols and materials databases

DNASUi 27429.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000258080 ; ENSP00000258080 ; ENSG00000115317 . [O43464-1 ]
ENST00000352222 ; ENSP00000312893 ; ENSG00000115317 . [O43464-2 ]
ENST00000437202 ; ENSP00000399166 ; ENSG00000115317 .
GeneIDi 27429.
KEGGi hsa:27429.
UCSCi uc002smi.1. human. [O43464-1 ]
uc002smj.1. human. [O43464-2 ]
uc002smk.1. human. [O43464-3 ]

Organism-specific databases

CTDi 27429.
GeneCardsi GC02P074757.
GeneReviewsi HTRA2.
HGNCi HGNC:14348. HTRA2.
HPAi CAB004004.
HPA027366.
MIMi 168600. phenotype.
606441. gene.
610297. phenotype.
neXtProti NX_O43464.
Orphaneti 2828. Young adult-onset Parkinsonism.
PharmGKBi PA33836.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0265.
GeneTreei ENSGT00510000046315.
HOGENOMi HOG000223641.
HOVERGENi HBG052044.
InParanoidi O43464.
KOi K08669.
OMAi FKEECTE.
OrthoDBi EOG7V1FR7.
PhylomeDBi O43464.
TreeFami TF323480.

Enzyme and pathway databases

BRENDAi 3.4.21.108. 2681.

Miscellaneous databases

ChiTaRSi HTRA2. human.
EvolutionaryTracei O43464.
GeneWikii HtrA_serine_peptidase_2.
GenomeRNAii 27429.
NextBioi 50463.
PMAP-CutDB O43464.
PROi O43464.
SOURCEi Search...

Gene expression databases

Bgeei O43464.
CleanExi HS_HTRA2.
Genevestigatori O43464.

Family and domain databases

Gene3Di 2.30.42.10. 1 hit.
InterProi IPR001478. PDZ.
IPR001254. Peptidase_S1.
IPR001940. Peptidase_S1C.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view ]
Pfami PF13180. PDZ_2. 1 hit.
[Graphical view ]
PRINTSi PR00834. PROTEASES2C.
SMARTi SM00228. PDZ. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view ]
SUPFAMi SSF50156. SSF50156. 1 hit.
SSF50494. SSF50494. 1 hit.
PROSITEi PS50106. PDZ. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of a novel human serine protease that has extensive homology to bacterial heat shock endoprotease HtrA and is regulated by kidney ischemia."
    Faccio L., Fusco C., Chen A., Martinotti S., Bonventre J.V., Zervos A.S.
    J. Biol. Chem. 275:2581-2588(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), MUTAGENESIS OF SER-306.
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 3 AND 4), CHARACTERIZATION.
    Tissue: Brain.
  3. "Tissue-specific splicing of Omi stress-regulated endoprotease leads to an inactive protease with a modified PDZ motif."
    Faccio L., Fusco C., Viel A., Zervos A.S.
    Genomics 68:343-347(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Tissue: Kidney.
  4. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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).
    Tissue: Brain.
  6. "A serine protease, HtrA2, is released from the mitochondria and interacts with XIAP, inducing cell death."
    Suzuki Y., Imai Y., Nakayama H., Takahashi K., Takio K., Takahashi R.
    Mol. Cell 8:613-621(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 134-458, INTERACTION WITH XIAP, MUTAGENESIS OF ALA-134.
  7. "Expression, purification, and functional analysis of the human serine protease HtrA2."
    Savopoulos J.W., Carter P.S., Turconi S., Pettman G.R., Karran E.H., Gray C.W., Ward R.V., Jenkins O., Creasy C.L.
    Protein Expr. Purif. 19:227-234(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  8. "Dual role of BRUCE as an antiapoptotic IAP and a chimeric E2/E3 ubiquitin ligase."
    Bartke T., Pohl C., Pyrowolakis G., Jentsch S.
    Mol. Cell 14:801-811(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH BIRC6/BRUCE.
  9. "THAP5 is a human cardiac-specific inhibitor of cell cycle that is cleaved by the proapoptotic Omi/HtrA2 protease during cell death."
    Balakrishnan M.P., Cilenti L., Mashak Z., Popat P., Alnemri E.S., Zervos A.S.
    Am. J. Physiol. 297:H643-H653(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH THAP5.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Structural insights into the pro-apoptotic function of mitochondrial serine protease HtrA2/Omi."
    Li W., Srinivasula S.M., Chai J., Li P., Wu J.W., Zhang Z., Alnemri E.S., Shi Y.
    Nat. Struct. Biol. 9:436-441(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 134-458, SUBUNIT.
  12. Cited for: VARIANT PARK13 SER-399, VARIANT SER-141, CHARACTERIZATION OF VARIANTS SER-141 AND SER-399.
  13. "Genetic variability in the mitochondrial serine protease HTRA2 contributes to risk for Parkinson disease."
    Bogaerts V., Nuytemans K., Reumers J., Pals P., Engelborghs S., Pickut B., Corsmit E., Peeters K., Schymkowitz J., De Deyn P.P., Cras P., Rousseau F., Theuns J., Van Broeckhoven C.
    Hum. Mutat. 29:832-840(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS PRO-72; SER-141 AND TRP-404, ASSOCIATION WITH INCREASED RISK OF PARKINSON DISEASE.

Entry informationi

Entry nameiHTRA2_HUMAN
AccessioniPrimary (citable) accession number: O43464
Secondary accession number(s): Q9HBZ4, Q9P0Y3, Q9P0Y4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: May 1, 2000
Last modified: November 26, 2014
This is version 163 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Peptidase families
    Classification of peptidase families and list of entries
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3