O43464 (HTRA2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	HTRA2
Synonyms:	OMI, PRSS25

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	458 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.8 Ref.9
Catalytic activity	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.
Subunit structure	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. Ref.6 Ref.8 Ref.9 Ref.11
Subcellular location	Mitochondrion intermembrane space. Mitochondrion membrane; Single-pass membrane protein Potential. 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.
Tissue specificity	Isoform 1 is ubiquitous. Isoform 2 is expressed predominantly in the kidney, colon and thyroid.
Domain	The mature N-terminus is involved in the interaction with XIAP. The PDZ domain mediates interaction with MXI2.
Post-translational modification	Autoproteolytically activated.
Involvement in disease	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. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.12 Ref.13
Sequence similarities	Belongs to the peptidase S1B family. Contains 1 PDZ (DHR) domain.

Ontologies

Keywords
Biological process	Apoptosis
Cellular component	Membrane Mitochondrion
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation Neurodegeneration Parkinson disease Parkinsonism
Domain	Transit peptide Transmembrane Transmembrane helix
Molecular function	Hydrolase Protease Serine protease
PTM	Zymogen
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	adult walking behavior Inferred from electronic annotation. Source: Compara cell cycle arrest Traceable author statement PubMed 18309324. Source: UniProtKB cellular response to growth factor stimulus Inferred from mutant phenotype PubMed 20125124. Source: UniProtKB ceramide metabolic process Inferred from electronic annotation. Source: Compara cleavage of cytoskeletal proteins involved in execution phase of apoptosis Traceable author statement PubMed 18309324. Source: UniProtKB forebrain development Inferred from electronic annotation. Source: Compara intrinsic apoptotic signaling pathway Inferred from electronic annotation. Source: Compara mitochondrion organization Inferred from electronic annotation. Source: Compara negative regulation of cell death Inferred from electronic annotation. Source: Compara neuron development Inferred from electronic annotation. Source: Compara pentacyclic triterpenoid metabolic process Inferred from electronic annotation. Source: Compara positive regulation of apoptotic process Inferred from mutant phenotype PubMed 20125124. Source: UniProtKB positive regulation of cysteine-type endopeptidase activity involved in apoptotic process Inferred from direct assay Ref.6PubMed 11604410. Source: UniProtKB positive regulation of intrinsic apoptotic signaling pathway Inferred from mutant phenotype PubMed 20125124. Source: UniProtKB regulation of multicellular organism growth Inferred from electronic annotation. Source: Compara response to herbicide Inferred from electronic annotation. Source: Compara response to stress Traceable author statement Ref.2. Source: UniProtKB
Cellular_component	CD40 receptor complex Inferred from sequence or structural similarity. Source: BHF-UCL cytosol Inferred from direct assay Ref.6PubMed 11604410. Source: UniProtKB endoplasmic reticulum membrane Traceable author statement Ref.1. Source: UniProtKB internal side of plasma membrane Inferred from sequence or structural similarity. Source: BHF-UCL mitochondrial intermembrane space Inferred from direct assay PubMed 15044455. Source: MGI mitochondrial membrane Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Traceable author statement Ref.2. Source: UniProtKB
Molecular_function	serine-type endopeptidase activity Traceable author statement Ref.7. Source: UniProtKB unfolded protein binding Non-traceable author statement Ref.1. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
BIRC7	Q96CA5	2	EBI-517086,EBI-517623
CSN2	P02666	2	EBI-517086,EBI-5260183	From a different organism.
NDUFA13	Q9P0J0	6	EBI-517086,EBI-372742
Ripk1	Q60855	2	EBI-517086,EBI-529119	From a different organism.
XIAP	P98170	10	EBI-517086,EBI-517127

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: O43464-1)

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.

Isoform 2 (identifier: O43464-2)

Also known as: D-Omi;

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

Isoform 3 (identifier: O43464-3)

Also known as: p7;

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

Isoform 4 (identifier: O43464-4)

Also known as: p4;

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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 31

31

Mitochondrion

Propeptide

32 – 133

102

PRO_0000026945

Chain

134 – 458

325

Serine protease HTRA2, mitochondrial

PRO_0000026946

Regions

Transmembrane

105 – 125

21

Helical; Potential

Domain

364 – 445

82

PDZ

Region

166 – 342

177

Serine protease

Motif

134 – 137

4

IAP-binding motif

Sites

Active site

198

1

Charge relay system

Active site

228

1

Charge relay system

Active site

306

1

Charge relay system

Natural variations

Alternative sequence

238 – 302

65

Missing in isoform 2.

VSP_005359

Alternative sequence

313

1

L → LARELGAVSLQ in isoform 3.

VSP_005360

Alternative sequence

314 – 458

145

DGEVI…PEVTE → VSETSFLPRIPAPGQCGKGR FPLIQGCLVKFLSSSLLAIS QYPTRSPQHLLVLLFGCPHP LLFV in isoform 4.

VSP_005362

Alternative sequence

372 – 403

32

Missing in isoform 2 and isoform 3.

VSP_005361

Natural variant

72

1

L → P. Ref.13

VAR_046134

Natural variant

141

1

A → S Polymorphism; associated with a 2.15-fold increased risk of PD; reduced protease activity. Ref.12 Ref.13

VAR_027349

Natural variant

399

1

G → S in PARK13; reduced protease activity. Ref.12

VAR_027350

Natural variant

404

1

R → W Could be associated with an increased risk of developing PD. Ref.13

VAR_046135

Experimental info

Mutagenesis

134

1

A → M: Loss of interaction with XIAP. Loss of inhibition of XIAP activity. Ref.6

Mutagenesis

306

1

S → A: Loss of protease activity. Ref.1

Secondary structure

1

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458

Helix Strand Turn

Details...

Helix

143 – 146

4

Helix

149 – 157

9

Helix

158 – 160

3

Beta strand

161 – 170

10

Turn

171 – 174

4

Beta strand

175 – 188

14

Turn

189 – 191

3

Beta strand

192 – 195

4

Helix

197 – 200

4

Beta strand

204 – 209

6

Beta strand

215 – 224

10

Turn

225 – 228

4

Beta strand

229 – 233

5

Helix

248 – 250

3

Beta strand

256 – 259

4

Beta strand

265 – 268

4

Beta strand

271 – 275

5

Beta strand

295 – 299

5

Turn

303 – 307

5

Beta strand

308 – 312

5

Beta strand

317 – 326

10

Beta strand

329 – 334

6

Helix

335 – 341

7

Beta strand

364 – 368

5

Helix

371 – 377

7

Beta strand

391 – 396

6

Helix

401 – 405

5

Beta strand

412 – 416

5

Helix

424 – 431

8

Beta strand

435 – 443

9

Beta strand

446 – 452

7

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (13B) [UniParc]. Last modified May 1, 2000. Version 2. Checksum: CEA955A7D0DD8C0D	FASTA	458	48,841
	10 20 30 40 50 60 MAAPRAGRGA GWSLRAWRAL GGIRWGRRPR LTPDLRALLT SGTSDPRARV TYGTPSLWAR 70 80 90 100 110 120 LSVGVTEPRA CLTSGTPGPR AQLTAVTPDT RTREASENSG TRSRAWLAVA LGAGGAVLLL 130 140 150 160 170 180 LWGGGRGPPA VLAAVPSPPP ASPRSQYNFI ADVVEKTAPA VVYIEILDRH PFLGREVPIS 190 200 210 220 230 240 NGSGFVVAAD GLIVTNAHVV ADRRRVRVRL LSGDTYEAVV TAVDPVADIA TLRIQTKEPL 250 260 270 280 290 300 PTLPLGRSAD VRQGEFVVAM GSPFALQNTI TSGIVSSAQR PARDLGLPQT NVEYIQTDAA 310 320 330 340 350 360 IDFGNSGGPL VNLDGEVIGV NTMKVTAGIS FAIPSDRLRE FLHRGEKKNS SSGISGSQRR 370 380 390 400 410 420 YIGVMMLTLS PSILAELQLR EPSFPDVQHG VLIHKVILGS PAHRAGLRPG DVILAIGEQM 430 440 450 VQNAEDVYEA VRTQSQLAVQ IRRGRETLTL YVTPEVTE
	Isoform 2 (D-Omi) [UniParc]. Checksum: BD0824D4308140D7	FASTA	361	38,493
	10 20 30 40 50 60 MAAPRAGRGA GWSLRAWRAL GGIRWGRRPR LTPDLRALLT SGTSDPRARV TYGTPSLWAR 70 80 90 100 110 120 LSVGVTEPRA CLTSGTPGPR AQLTAVTPDT RTREASENSG TRSRAWLAVA LGAGGAVLLL 130 140 150 160 170 180 LWGGGRGPPA VLAAVPSPPP ASPRSQYNFI ADVVEKTAPA VVYIEILDRH PFLGREVPIS 190 200 210 220 230 240 NGSGFVVAAD GLIVTNAHVV ADRRRVRVRL LSGDTYEAVV TAVDPVADIA TLRIQTKFGN 250 260 270 280 290 300 SGGPLVNLDG EVIGVNTMKV TAGISFAIPS DRLREFLHRG EKKNSSSGIS GSQRRYIGVM 310 320 330 340 350 360 MLTLSPRAGL RPGDVILAIG EQMVQNAEDV YEAVRTQSQL AVQIRRGRET LTLYVTPEVT E
	Isoform 3 (p7) [UniParc]. Checksum: B48266A8EB7E4EE8	FASTA	436	46,382
	10 20 30 40 50 60 MAAPRAGRGA GWSLRAWRAL GGIRWGRRPR LTPDLRALLT SGTSDPRARV TYGTPSLWAR 70 80 90 100 110 120 LSVGVTEPRA CLTSGTPGPR AQLTAVTPDT RTREASENSG TRSRAWLAVA LGAGGAVLLL 130 140 150 160 170 180 LWGGGRGPPA VLAAVPSPPP ASPRSQYNFI ADVVEKTAPA VVYIEILDRH PFLGREVPIS 190 200 210 220 230 240 NGSGFVVAAD GLIVTNAHVV ADRRRVRVRL LSGDTYEAVV TAVDPVADIA TLRIQTKEPL 250 260 270 280 290 300 PTLPLGRSAD VRQGEFVVAM GSPFALQNTI TSGIVSSAQR PARDLGLPQT NVEYIQTDAA 310 320 330 340 350 360 IDFGNSGGPL VNLARELGAV SLQDGEVIGV NTMKVTAGIS FAIPSDRLRE FLHRGEKKNS 370 380 390 400 410 420 SSGISGSQRR YIGVMMLTLS PRAGLRPGDV ILAIGEQMVQ NAEDVYEAVR TQSQLAVQIR 430 RGRETLTLYV TPEVTE
	Isoform 4 (p4) [UniParc]. Checksum: 14D0982E08A58FB2	FASTA	377	39,914
	10 20 30 40 50 60 MAAPRAGRGA GWSLRAWRAL GGIRWGRRPR LTPDLRALLT SGTSDPRARV TYGTPSLWAR 70 80 90 100 110 120 LSVGVTEPRA CLTSGTPGPR AQLTAVTPDT RTREASENSG TRSRAWLAVA LGAGGAVLLL 130 140 150 160 170 180 LWGGGRGPPA VLAAVPSPPP ASPRSQYNFI ADVVEKTAPA VVYIEILDRH PFLGREVPIS 190 200 210 220 230 240 NGSGFVVAAD GLIVTNAHVV ADRRRVRVRL LSGDTYEAVV TAVDPVADIA TLRIQTKEPL 250 260 270 280 290 300 PTLPLGRSAD VRQGEFVVAM GSPFALQNTI TSGIVSSAQR PARDLGLPQT NVEYIQTDAA 310 320 330 340 350 360 IDFGNSGGPL VNLVSETSFL PRIPAPGQCG KGRFPLIQGC LVKFLSSSLL AISQYPTRSP 370 QHLLVLLFGC PHPLLFV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"Characterization of human HtrA2, a novel serine protease involved in the mammalian cellular stress response." Gray C.W., Ward R.V., Karran E.H., Turconi S., Rowles A., Viglienghi D., Southan C., Barton A., Fantom K.G., West A., Savopoulos J.W., Hassan N.J., Clinkenbeard H., Hanning C., Amegadzie B., Davis J.B., Dingwall C., Livi G.P., Creasy C.L. Eur. J. Biochem. 267:5699-5710(2000) [PubMed] [Europe PMC] [Abstract] 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]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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]	"Loss of function mutations in the gene encoding Omi/HtrA2 in Parkinson's disease." Strauss K.M., Martins L.M., Plun-Favreau H., Marx F.P., Kautzmann S., Berg D., Gasser T., Wszolek Z., Mueller T., Bornemann A., Wolburg H., Downward J., Riess O., Schulz J.B., Krueger R. Hum. Mol. Genet. 14:2099-2111(2005) [PubMed] [Europe PMC] [Abstract] 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.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00001663.
IPI00220542.
IPI00220543.
IPI00220544.

RefSeq

NP_037379.1. NM_013247.4.
NP_659540.1. NM_145074.2.

UniGene

Hs.469045.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1LCY	X-ray	2.00	A	134-458	[»]
2PZD	X-ray	2.75	A/B	359-458	[»]

DisProt

DP00315.

ProteinModelPortal

O43464.

ModBase

Search...

Protein-protein interaction databases

IntAct

O43464. 38 interactions.

MINT

MINT-216075.

STRING

9606.ENSP00000258080.

Protein family/group databases

MEROPS

S01.278.

PTM databases

PhosphoSite

O43464.

2D gel databases

OGP

O43464.

Proteomic databases

PaxDb

O43464.

PRIDE

O43464.

Protocols and materials databases

DNASU

27429.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000258080; ENSP00000258080; ENSG00000115317.
ENST00000352222; ENSP00000312893; ENSG00000115317.
ENST00000437202; ENSP00000399166; ENSG00000115317.

GeneID

27429.

KEGG

hsa:27429.

UCSC

uc002smi.1. human.
uc002smj.1. human.
uc002smk.1. human.

Organism-specific databases

CTD

27429.

GeneCards

GC02P074757.

HGNC

HGNC:14348. HTRA2.

HPA

CAB004004.
HPA027366.

MIM

168600. phenotype.
606441. gene.
610297. phenotype.

neXtProt

NX_O43464.

Orphanet

2828. Young adult-onset Parkinsonism.

PharmGKB

PA33836.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0265.

HOGENOM

HOG000223641.

HOVERGEN

HBG052044.

InParanoid

O43464.

KO

K08669.

OMA

CLTSGTP.

OrthoDB

EOG4J9N00.

PhylomeDB

O43464.

Enzyme and pathway databases

BRENDA

3.4.21.108. 2681.

Gene expression databases

Bgee

O43464.

CleanEx

HS_HTRA2.

Genevestigator

O43464.

GermOnline

ENSG00000115317. Homo sapiens.

Family and domain databases

InterPro

IPR001478. PDZ.
IPR001254. Peptidase_S1.
IPR001940. Peptidase_S1C.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]

Pfam

PF13180. PDZ_2. 1 hit.
[Graphical view]

PRINTS

PR00834. PROTEASES2C.

SMART

SM00228. PDZ. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]

SUPFAM

SSF50156. PDZ. 1 hit.
SSF50494. Pept_Ser_Cys. 1 hit.

PROSITE

PS50106. PDZ. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

HTRA2. human.

EvolutionaryTrace

O43464.

GenomeRNAi

27429.

NextBio

50463.

PMAP-CutDB

O43464.

SOURCE

Search...

Entry information

Entry name

HTRA2_HUMAN

Accession

Primary (citable) accession number: O43464
Secondary accession number(s): Q9HBZ4, Q9P0Y3, Q9P0Y4

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 26, 2001
Last sequence update:	May 1, 2000
Last modified:	May 29, 2013
This is version 148 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.