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O43464 (HTRA2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 159. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length458 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 processApoptosis
   Cellular componentMembrane
Mitochondrion
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
Neurodegeneration
Parkinson disease
Parkinsonism
   DomainTransit peptide
Transmembrane
Transmembrane helix
   Molecular functionHydrolase
Protease
Serine protease
   PTMZymogen
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processadult walking behavior

Inferred from electronic annotation. Source: Ensembl

cellular response to growth factor stimulus

Inferred from mutant phenotype PubMed 20125124. Source: UniProtKB

cellular response to heat

Inferred from direct assay Ref.2. Source: UniProtKB

ceramide metabolic process

Inferred from electronic annotation. Source: Ensembl

execution phase of apoptosis

Traceable author statement PubMed 18309324. Source: UniProtKB

forebrain development

Inferred from electronic annotation. Source: Ensembl

intrinsic apoptotic signaling pathway in response to DNA damage

Inferred from mutant phenotype PubMed 11602612. Source: ParkinsonsUK-UCL

mitochondrion organization

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell cycle

Traceable author statement PubMed 18309324. Source: UniProtKB

negative regulation of cell death

Inferred from electronic annotation. Source: Ensembl

neuron development

Inferred from electronic annotation. Source: Ensembl

pentacyclic triterpenoid metabolic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of apoptotic process

Inferred from mutant phenotype PubMed 20125124. Source: UniProtKB

positive regulation of cell death

Inferred from direct assay Ref.6. 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 cysteine-type endopeptidase activity involved in apoptotic signaling pathway

Inferred from mutant phenotype PubMed 11602612. Source: ParkinsonsUK-UCL

positive regulation of extrinsic apoptotic signaling pathway in absence of ligand

Inferred from mutant phenotype PubMed 20125124. Source: UniProtKB

protein autoprocessing

Traceable author statement PubMed 11602612. Source: ParkinsonsUK-UCL

proteolysis

Inferred from mutant phenotype Ref.2. Source: UniProtKB

regulation of multicellular organism growth

Inferred from electronic annotation. Source: Ensembl

response to herbicide

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentCD40 receptor complex

Inferred from sequence or structural similarity. Source: BHF-UCL

cytoplasmic side of plasma membrane

Inferred from sequence or structural similarity. Source: BHF-UCL

cytosol

Inferred from direct assay PubMed 11602612. Source: ParkinsonsUK-UCL

endoplasmic reticulum

Non-traceable author statement Ref.3. Source: UniProtKB

endoplasmic reticulum membrane

Traceable author statement Ref.1. Source: UniProtKB

mitochondrial intermembrane space

Inferred from direct assay PubMed 15044455. Source: MGI

mitochondrial membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

mitochondrion

Inferred from direct assay Ref.6. Source: UniProtKB

nucleus

Inferred from direct assay Ref.2. Source: UniProtKB

   Molecular_functionpeptidase activity

Inferred from direct assay PubMed 11604410PubMed 17266347PubMed 20125124. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.8Ref.9. Source: UniProtKB

serine-type endopeptidase activity

Inferred from mutant phenotype Ref.2. Source: UniProtKB

serine-type peptidase activity

Inferred from direct assay Ref.6. Source: UniProtKB

unfolded protein binding

Non-traceable author statement Ref.1. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

BIRC7Q96CA52EBI-517086,EBI-517623
CSN2P026662EBI-517086,EBI-5260183From a different organism.
NDUFA13Q9P0J06EBI-517086,EBI-372742
Ripk1Q608552EBI-517086,EBI-529119From a different organism.
XIAPP981708EBI-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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3131Mitochondrion
Propeptide32 – 133102
PRO_0000026945
Chain134 – 458325Serine protease HTRA2, mitochondrial
PRO_0000026946

Regions

Transmembrane105 – 12521Helical; Potential
Domain364 – 44582PDZ
Region166 – 342177Serine protease
Motif134 – 1374IAP-binding motif

Sites

Active site1981Charge relay system
Active site2281Charge relay system
Active site3061Charge relay system

Natural variations

Alternative sequence238 – 30265Missing in isoform 2.
VSP_005359
Alternative sequence3131L → LARELGAVSLQ in isoform 3.
VSP_005360
Alternative sequence314 – 458145DGEVI…PEVTE → VSETSFLPRIPAPGQCGKGR FPLIQGCLVKFLSSSLLAIS QYPTRSPQHLLVLLFGCPHP LLFV in isoform 4.
VSP_005362
Alternative sequence372 – 40332Missing in isoform 2 and isoform 3.
VSP_005361
Natural variant721L → P. Ref.13
Corresponds to variant rs150047108 [ dbSNP | Ensembl ].
VAR_046134
Natural variant1411A → S Polymorphism; associated with a 2.15-fold increased risk of PD; reduced protease activity. Ref.12 Ref.13
Corresponds to variant rs72470544 [ dbSNP | Ensembl ].
VAR_027349
Natural variant3991G → S in PARK13; reduced protease activity. Ref.12
Corresponds to variant rs72470545 [ dbSNP | Ensembl ].
VAR_027350
Natural variant4041R → W Could be associated with an increased risk of developing PD. Ref.13
VAR_046135

Experimental info

Mutagenesis1341A → M: Loss of interaction with XIAP. Loss of inhibition of XIAP activity. Ref.6
Mutagenesis3061S → A: Loss of protease activity. Ref.1

Secondary structure

..................................................... 458
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (13B) [UniParc].

Last modified May 1, 2000. Version 2.
Checksum: CEA955A7D0DD8C0D

FASTA45848,841
        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 

« Hide

Isoform 2 (D-Omi) [UniParc].

Checksum: BD0824D4308140D7
Show »

FASTA36138,493
Isoform 3 (p7) [UniParc].

Checksum: B48266A8EB7E4EE8
Show »

FASTA43646,382
Isoform 4 (p4) [UniParc].

Checksum: 14D0982E08A58FB2
Show »

FASTA37739,914

References

« Hide '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. expand/collapse author list , 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.

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.
CCDSCCDS1951.1. [O43464-1]
CCDS1952.1. [O43464-2]
RefSeqNP_037379.1. NM_013247.4. [O43464-1]
NP_659540.1. NM_145074.2. [O43464-2]
UniGeneHs.469045.
Hs.744841.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1LCYX-ray2.00A134-458[»]
2PZDX-ray2.75A/B359-458[»]
DisProtDP00315.
ProteinModelPortalO43464.
SMRO43464. Positions 139-458.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid118165. 47 interactions.
IntActO43464. 37 interactions.
MINTMINT-216075.
STRING9606.ENSP00000258080.

Protein family/group databases

MEROPSS01.278.

PTM databases

PhosphoSiteO43464.

2D gel databases

OGPO43464.

Proteomic databases

MaxQBO43464.
PaxDbO43464.
PRIDEO43464.

Protocols and materials databases

DNASU27429.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000258080; ENSP00000258080; ENSG00000115317. [O43464-1]
ENST00000352222; ENSP00000312893; ENSG00000115317. [O43464-2]
ENST00000437202; ENSP00000399166; ENSG00000115317.
GeneID27429.
KEGGhsa:27429.
UCSCuc002smi.1. human. [O43464-1]
uc002smj.1. human. [O43464-2]
uc002smk.1. human. [O43464-3]

Organism-specific databases

CTD27429.
GeneCardsGC02P074757.
GeneReviewsHTRA2.
HGNCHGNC:14348. HTRA2.
HPACAB004004.
HPA027366.
MIM168600. phenotype.
606441. gene.
610297. phenotype.
neXtProtNX_O43464.
Orphanet2828. Young adult-onset Parkinsonism.
PharmGKBPA33836.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0265.
HOGENOMHOG000223641.
HOVERGENHBG052044.
InParanoidO43464.
KOK08669.
OMAFKEECTE.
OrthoDBEOG7V1FR7.
PhylomeDBO43464.
TreeFamTF323480.

Enzyme and pathway databases

BRENDA3.4.21.108. 2681.

Gene expression databases

BgeeO43464.
CleanExHS_HTRA2.
GenevestigatorO43464.

Family and domain databases

Gene3D2.30.42.10. 1 hit.
InterProIPR001478. PDZ.
IPR001254. Peptidase_S1.
IPR001940. Peptidase_S1C.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamPF13180. PDZ_2. 1 hit.
[Graphical view]
PRINTSPR00834. PROTEASES2C.
SMARTSM00228. PDZ. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMSSF50156. SSF50156. 1 hit.
SSF50494. SSF50494. 1 hit.
PROSITEPS50106. PDZ. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSHTRA2. human.
EvolutionaryTraceO43464.
GeneWikiHtrA_serine_peptidase_2.
GenomeRNAi27429.
NextBio50463.
PMAP-CutDBO43464.
PROO43464.
SOURCESearch...

Entry information

Entry nameHTRA2_HUMAN
AccessionPrimary (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: July 9, 2014
This is version 159 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM