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P30048 (PRDX3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 170. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | 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:
Thioredoxin-dependent peroxide reductase, mitochondrial

EC=1.11.1.15
Alternative name(s):
Antioxidant protein 1
Short name=AOP-1
HBC189
Peroxiredoxin III
Short name=Prx-III
Peroxiredoxin-3
Protein MER5 homolog
Gene names
Name:PRDX3
Synonyms:AOP1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length256 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in redox regulation of the cell. Protects radical-sensitive enzymes from oxidative damage by a radical-generating system. Acts synergistically with MAP3K13 to regulate the activation of NF-kappa-B in the cytosol. Ref.12

Catalytic activity

2 R'-SH + ROOH = R'-S-S-R' + H2O + ROH.

Subunit structure

Dodecameric ring assembled from homodimeric units; disulfide-linked, upon oxidation. The rings have an approximate diameter of 150 A and a central hole of 70 A. 3-5% of the rings are interlocked by pairs. Binds MAP3K13. Interacts with NEK6. Interacts with LRRK2. Ref.12 Ref.13 Ref.15 Ref.17

Subcellular location

Mitochondrion.

Post-translational modification

Phosphorylated by LRRK2; phosphorylation reduces perodixase activity. Ref.17

Miscellaneous

The active site is the redox-active Cys-108 oxidized to Cys-SOH. Cys-SOH rapidly reacts with Cys-229-SH of the other subunit to form an intermolecular disulfide with a concomitant homodimer formation. The enzyme may be subsequently regenerated by reduction of the disulfide by thioredoxin.

Irreversibly inactivated by overoxidation of Cys-108 (to Cys-SO3H) upon oxidative stress.

Sequence similarities

Belongs to the AhpC/TSA family.

Contains 1 thioredoxin domain.

Ontologies

Keywords
   Cellular componentMitochondrion
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRedox-active center
Transit peptide
   Molecular functionAntioxidant
Oxidoreductase
Peroxidase
   PTMAcetylation
Disulfide bond
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcellular response to reactive oxygen species

Inferred from mutant phenotype PubMed 18262354. Source: UniProtKB

hydrogen peroxide catabolic process

Inferred from mutant phenotype PubMed 18195003. Source: UniProtKB

maternal placenta development

Inferred from electronic annotation. Source: Ensembl

mitochondrion organization

Inferred from mutant phenotype PubMed 12011429. Source: UniProtKB

myeloid cell differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of apoptotic process

Inferred from mutant phenotype PubMed 18262354. Source: UniProtKB

negative regulation of cysteine-type endopeptidase activity involved in apoptotic process

Inferred from mutant phenotype PubMed 18262354. Source: GOC

negative regulation of kinase activity

Inferred from direct assay PubMed 18205602. Source: UniProtKB

positive regulation of NF-kappaB transcription factor activity

Inferred from direct assay Ref.12. Source: UniProtKB

positive regulation of cell proliferation

Inferred from direct assay PubMed 12011429. Source: UniProtKB

regulation of mitochondrial membrane potential

Inferred from mutant phenotype PubMed 12011429. Source: UniProtKB

response to hydrogen peroxide

Inferred from direct assay PubMed 17893648. Source: UniProtKB

response to lipopolysaccharide

Inferred from sequence or structural similarity. Source: UniProtKB

response to oxidative stress

Inferred from mutant phenotype PubMed 18195003. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 18205602. Source: UniProtKB

early endosome

Inferred from direct assay PubMed 15750338. Source: UniProtKB

mitochondrial matrix

Traceable author statement. Source: Reactome

mitochondrion

Inferred from direct assay PubMed 17893648PubMed 18262354. Source: UniProtKB

   Molecular_functionalkyl hydroperoxide reductase activity

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

cysteine-type endopeptidase inhibitor activity involved in apoptotic process

Inferred from mutant phenotype PubMed 18262354. Source: UniProtKB

kinase binding

Inferred from physical interaction PubMed 18205602. Source: UniProtKB

peroxidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

peroxiredoxin activity

Inferred from electronic annotation. Source: UniProtKB-EC

protein C-terminus binding

Inferred from physical interaction PubMed 17060495. Source: UniProtKB

protein kinase binding

Inferred from physical interaction Ref.12. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

LRRK2Q5S00710EBI-748336,EBI-5323863

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P30048-1)

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: P30048-2)

The sequence of this isoform differs from the canonical sequence as follows:
     51-68: Missing.
Note: No experimental confirmation available. Gene prediction based on EST data.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 6262Mitochondrion Ref.9
Chain63 – 256194Thioredoxin-dependent peroxide reductase, mitochondrial
PRO_0000023782

Regions

Domain63 – 221159Thioredoxin

Sites

Active site1081Cysteine sulfenic acid (-SOH) intermediate By similarity

Amino acid modifications

Modified residue831N6-succinyllysine By similarity
Modified residue911N6-acetyllysine; alternate Ref.14
Modified residue911N6-succinyllysine; alternate By similarity
Modified residue1461Phosphothreonine Probable
Disulfide bond108Interchain (with C-229); in linked form By similarity
Disulfide bond229Interchain (with C-108); in linked form By similarity

Natural variations

Alternative sequence51 – 6818Missing in isoform 2.
VSP_054050
Natural variant551S → R. Ref.5
Corresponds to variant rs34698541 [ dbSNP | Ensembl ].
VAR_025052
Natural variant1701R → Q.
Corresponds to variant rs11554902 [ dbSNP | Ensembl ].
VAR_059546
Natural variant2181A → T. Ref.5
VAR_025053
Natural variant2341T → I. Ref.5
Corresponds to variant rs35697338 [ dbSNP | Ensembl ].
VAR_025054

Experimental info

Mutagenesis1461T → A: Impairs phosphorylation. Ref.17
Sequence conflict311R → W in AAH08435. Ref.8

Sequences

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

Last modified November 1, 1997. Version 3.
Checksum: 8BEB7F5E55BFE9BE

FASTA25627,693
        10         20         30         40         50         60 
MAAAVGRLLR ASVARHVSAI PWGISATAAL RPAACGRTSL TNLLCSGSSQ AKLFSTSSSC 

        70         80         90        100        110        120 
HAPAVTQHAP YFKGTAVVNG EFKDLSLDDF KGKYLVLFFY PLDFTFVCPT EIVAFSDKAN 

       130        140        150        160        170        180 
EFHDVNCEVV AVSVDSHFSH LAWINTPRKN GGLGHMNIAL LSDLTKQISR DYGVLLEGSG 

       190        200        210        220        230        240 
LALRGLFIID PNGVIKHLSV NDLPVGRSVE ETLRLVKAFQ YVETHGEVCP ANWTPDSPTI 

       250 
KPSPAASKEY FQKVNQ 

« Hide

Isoform 2 [UniParc].

Checksum: 28657F36943A2355
Show »

FASTA23825,839

References

« Hide 'large scale' references
[1]"Mammalian antioxidant protein complements alkylhydroperoxide reductase (ahpC) mutation in Escherichia coli."
Tsuji K., Copeland N.G., Jenkins N.A., Obinata M.
Biochem. J. 307:377-381(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Blood.
[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. expand/collapse author list , 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] (ISOFORM 1).
Tissue: Lung.
[3]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[4]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[5]NIEHS SNPs program
Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ARG-55; THR-218 AND ILE-234.
[6]"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. expand/collapse author list , 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].
[7]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"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: Bone marrow, Skeletal muscle, Testis, Urinary bladder and Uterus.
[9]"Human liver protein map: a reference database established by microsequencing and gel comparison."
Hochstrasser D.F., Frutiger S., Paquet N., Bairoch A., Ravier F., Pasquali C., Sanchez J.-C., Tissot J.-D., Bjellqvist B., Vargas R., Appel R.D., Hughes G.J.
Electrophoresis 13:992-1001(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 63-72 (ISOFORM 1).
Tissue: Liver.
[10]Lubec G., Vishwanath V., Chen W.-Q., Sun Y.
Submitted (DEC-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 74-93; 149-166 AND 171-214 (ISOFORM 1), IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[11]"A method for detection of overoxidation of cysteines: peroxiredoxins are oxidized in vivo at the active-site cysteine during oxidative stress."
Wagner E., Luche S., Penna L., Chevallet M., van Dorsselaer A., Leize-Wagner E., Rabilloud T.
Biochem. J. 366:777-785(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: OVEROXIDATION AT CYS-108.
[12]"Mixed lineage kinase LZK and antioxidant protein-1 activate NF-kappaB synergistically."
Masaki M., Ikeda A., Shiraki E., Oka S., Kawasaki T.
Eur. J. Biochem. 270:76-83(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH MAP3K13.
[13]"Reconstitution of the mitochondrial PrxIII antioxidant defence pathway: general properties and factors affecting PrxIII activity and oligomeric state."
Cao Z., Bhella D., Lindsay J.G.
J. Mol. Biol. 372:1022-1033(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT.
[14]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-91, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"Characterization of hNek6 interactome reveals an important role for its short N-terminal domain and colocalization with proteins at the centrosome."
Vaz Meirelles G., Ferreira Lanza D.C., da Silva J.C., Santana Bernachi J., Paes Leme A.F., Kobarg J.
J. Proteome Res. 9:6298-6316(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NEK6.
[16]"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].
[17]"Mutations in LRRK2 increase phosphorylation of peroxiredoxin 3 exacerbating oxidative stress-induced neuronal death."
Angeles D.C., Gan B.H., Onstead L., Zhao Y., Lim K.L., Dachsel J., Melrose H., Farrer M., Wszolek Z.K., Dickson D.W., Tan E.K.
Hum. Mutat. 32:1390-1397(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH LRRK2, PHOSPHORYLATION AT THR-146, MUTAGENESIS OF THR-146.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D49396 mRNA. Translation: BAA08389.1.
AK313169 mRNA. Translation: BAG35987.1.
CR450344 mRNA. Translation: CAG29340.1.
BT020007 mRNA. Translation: AAV38810.1.
DQ298752 Genomic DNA. Translation: ABB84468.1.
AL355861 Genomic DNA. Translation: CAI15802.1.
CH471066 Genomic DNA. Translation: EAW49399.1.
BC002685 mRNA. Translation: AAH02685.1.
BC007062 mRNA. Translation: AAH07062.1.
BC008435 mRNA. Translation: AAH08435.1.
BC009601 mRNA. Translation: AAH09601.1.
BC021691 mRNA. Translation: AAH21691.1.
BC022373 mRNA. Translation: AAH22373.1.
BC059169 mRNA. Translation: AAH59169.1.
BC111397 mRNA. Translation: AAI11398.1.
RefSeqNP_006784.1. NM_006793.3.
NP_054817.2. NM_014098.3.
UniGeneHs.523302.

3D structure databases

ProteinModelPortalP30048.
SMRP30048. Positions 63-223.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116136. 41 interactions.
IntActP30048. 34 interactions.
MINTMINT-195453.
STRING9606.ENSP00000298510.

Protein family/group databases

PeroxiBase4492. Hs2CysPrx03.

PTM databases

PhosphoSiteP30048.

Polymorphism databases

DMDM2507171.

2D gel databases

OGPP30048.
SWISS-2DPAGEP30048.
UCD-2DPAGEP30048.

Proteomic databases

PaxDbP30048.
PeptideAtlasP30048.
PRIDEP30048.

Protocols and materials databases

DNASU10935.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000298510; ENSP00000298510; ENSG00000165672.
ENST00000356951; ENSP00000349432; ENSG00000165672.
GeneID10935.
KEGGhsa:10935.
UCSCuc001lec.3. human.

Organism-specific databases

CTD10935.
GeneCardsGC10M120917.
H-InvDBHIX0035477.
HGNCHGNC:9354. PRDX3.
HPACAB008656.
MIM604769. gene.
neXtProtNX_P30048.
PharmGKBPA33724.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0450.
HOVERGENHBG000286.
InParanoidP30048.
KOK03386.
OMAFAHKAWH.
OrthoDBEOG7T1RCD.
PhylomeDBP30048.
TreeFamTF105181.

Enzyme and pathway databases

ReactomeREACT_120956. Cellular responses to stress.

Gene expression databases

ArrayExpressP30048.
BgeeP30048.
CleanExHS_PRDX3.
GenevestigatorP30048.

Family and domain databases

Gene3D3.40.30.10. 1 hit.
InterProIPR000866. AhpC/TSA.
IPR024706. Peroxiredoxin_AhpC-typ.
IPR019479. Peroxiredoxin_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamPF10417. 1-cysPrx_C. 1 hit.
PF00578. AhpC-TSA. 1 hit.
[Graphical view]
PIRSFPIRSF000239. AHPC. 1 hit.
SUPFAMSSF52833. SSF52833. 1 hit.
PROSITEPS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPRDX3. human.
GeneWikiPRDX3.
GenomeRNAi10935.
NextBio41537.
PROP30048.
SOURCESearch...

Entry information

Entry namePRDX3_HUMAN
AccessionPrimary (citable) accession number: P30048
Secondary accession number(s): B2R7Z0 expand/collapse secondary AC list , D3DRC9, E9PH29, P35690, Q0D2H1, Q13776, Q5T5V2, Q96HK4
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: November 1, 1997
Last modified: April 16, 2014
This is version 170 of the entry and version 3 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

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 10

Human chromosome 10: entries, gene names and cross-references to MIM