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Q92874 (DNSL2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 121. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Deoxyribonuclease-1-like 2

EC=3.1.21.-
Alternative name(s):
DNase I homolog protein DHP1
Deoxyribonuclease I-like 2
Short name=DNase I-like 2
Gene names
Name:DNASE1L2
Synonyms:DHP1, DNAS1L2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length299 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Divalent cation-dependent acid DNA endonuclease involved in the breakdown of the nucleus during corneocyte formation of epidermal keratinocytes. May play an immune role by eliminating harmful DNA released into the extracellular environment by damaged epidermal cells. Ref.7

Cofactor

Divalent metal cations. Seems to require both calcium and magnesium. Ref.2

Subcellular location

Cytoplasm. Secreted Potential Ref.7.

Tissue specificity

Preferentially expressed in the skin and up-regulated during keratinocytes differentiation. Highly abundant (at protein level) in the stratum granulosum. Ref.7

Induction

Up-regulated by inflammatory cytokines. Ref.2

Sequence similarities

Belongs to the DNase I family.

Ontologies

Keywords
   Cellular componentCytoplasm
Secreted
   Coding sequence diversityAlternative splicing
   DomainSignal
   LigandMetal-binding
   Molecular functionEndonuclease
Hydrolase
Nuclease
   PTMDisulfide bond
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA metabolic process

Traceable author statement Ref.1. Source: ProtInc

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionDNA binding

Traceable author statement Ref.1. Source: ProtInc

calcium ion binding

Traceable author statement Ref.1. Source: ProtInc

deoxyribonuclease activity

Traceable author statement Ref.1. Source: ProtInc

endodeoxyribonuclease activity, producing 5'-phosphomonoesters

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q92874-1)

Also known as: DNAS1L2-L;

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: Q92874-2)

Also known as: DNAS1L2-S;

The sequence of this isoform differs from the canonical sequence as follows:
     140-160: Missing.
Note: Specifically expressed in peripheral blood leukocytes.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Chain21 – 299279Deoxyribonuclease-1-like 2
PRO_0000007286

Sites

Active site991 By similarity
Active site1701 By similarity

Amino acid modifications

Disulfide bond209 ↔ 245Essential for enzymatic activity By similarity

Natural variations

Alternative sequence140 – 16021Missing in isoform 2.
VSP_053879

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (DNAS1L2-L) [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: 1B66A5590D33D0A6

FASTA29932,853
        10         20         30         40         50         60 
MGGPRALLAA LWALEAAGTA ALRIGAFNIQ SFGDSKVSDP ACGSIIAKIL AGYDLALVQE 

        70         80         90        100        110        120 
VRDPDLSAVS ALMEQINSVS EHEYSFVSSQ PLGRDQYKEM YLFVYRKDAV SVVDTYLYPD 

       130        140        150        160        170        180 
PEDVFSREPF VVKFSAPGTG ERAPPLPSRR ALTPPPLPAA AQNLVLIPLH AAPHQAVAEI 

       190        200        210        220        230        240 
DALYDVYLDV IDKWGTDDML FLGDFNADCS YVRAQDWAAI RLRSSEVFKW LIPDSADTTV 

       250        260        270        280        290 
GNSDCAYDRI VACGARLRRS LKPQSATVHD FQEEFGLDQT QALAISDHFP VEVTLKFHR 

« Hide

Isoform 2 (DNAS1L2-S) [UniParc].

Checksum: 076B44856A08D0BE
Show »

FASTA27830,707

References

« Hide 'large scale' references
[1]"Identification, localization, and expression of two novel human genes similar to deoxyribonuclease I."
Rodriguez A.M., Rodin D., Nomura H., Morton C.C., Weremowicz S., Schneider M.C.
Genomics 42:507-513(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Characterization of the human DNAS1L2 gene and the molecular mechanism for its transcriptional activation induced by inflammatory cytokines."
Shiokawa D., Matsushita T., Kobayashi T., Matsumoto Y., Tanuma S.I.
Genomics 84:95-105(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), INDUCTION, COFACTOR, ALTERNATIVE SPLICING.
[3]"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].
Tissue: Thymus.
[4]"The sequence and analysis of duplication-rich human chromosome 16."
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J. expand/collapse author list , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Mural R.J., Istrail S., Sutton 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].
[6]"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: Skin.
[7]"DNase1L2 degrades nuclear DNA during corneocyte formation."
Fischer H., Eckhart L., Mildner M., Jaeger K., Buchberger M., Ghannadan M., Tschachler E.
J. Invest. Dermatol. 127:24-30(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U62647 mRNA. Translation: AAB63981.1.
AY298957 mRNA. Translation: AAQ73759.1.
AY298958 Genomic DNA. Translation: AAQ73760.1.
AY298958 Genomic DNA. Translation: AAQ73761.1.
AK098028 mRNA. Translation: BAG53566.1.
AC009065 Genomic DNA. No translation available.
CH471112 Genomic DNA. Translation: EAW85526.1.
CH471112 Genomic DNA. Translation: EAW85527.1.
CH471112 Genomic DNA. Translation: EAW85528.1.
CH471112 Genomic DNA. Translation: EAW85529.1.
BC035205 mRNA. Translation: AAH35205.1.
BC063710 mRNA. Translation: AAH63710.1.
RefSeqNP_001365.1. NM_001374.2.
XP_005255209.1. XM_005255152.2.
UniGeneHs.103503.

3D structure databases

ProteinModelPortalQ92874.
SMRQ92874. Positions 22-296.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ92874. 2 interactions.
MINTMINT-4722563.
STRING9606.ENSP00000316938.

Polymorphism databases

DMDM2494172.

Proteomic databases

PaxDbQ92874.
PRIDEQ92874.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000320700; ENSP00000316938; ENSG00000167968.
ENST00000382437; ENSP00000371874; ENSG00000167968.
ENST00000564065; ENSP00000454562; ENSG00000167968.
ENST00000567494; ENSP00000455358; ENSG00000167968.
GeneID1775.
KEGGhsa:1775.
UCSCuc002cpo.3. human. [Q92874-1]

Organism-specific databases

CTD1775.
GeneCardsGC16P002285.
H-InvDBHIX0038772.
HGNCHGNC:2958. DNASE1L2.
HPAHPA044714.
MIM602622. gene.
neXtProtNX_Q92874.
PharmGKBPA27429.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG46375.
HOGENOMHOG000059570.
HOVERGENHBG051368.
InParanoidQ92874.
KOK11995.
OMAYQYPDPE.
OrthoDBEOG73V6KW.
PhylomeDBQ92874.
TreeFamTF329541.

Gene expression databases

ArrayExpressQ92874.
BgeeQ92874.
CleanExHS_DNASE1L2.
GenevestigatorQ92874.

Family and domain databases

Gene3D3.60.10.10. 1 hit.
InterProIPR018057. Deoxyribonuclease-1_AS.
IPR016202. DNase_I.
IPR005135. Endo/exonuclease/phosphatase.
[Graphical view]
PANTHERPTHR11371. PTHR11371. 1 hit.
PfamPF03372. Exo_endo_phos. 1 hit.
[Graphical view]
PIRSFPIRSF000988. DNase_I_euk. 1 hit.
PRINTSPR00130. DNASEI.
SMARTSM00476. DNaseIc. 1 hit.
[Graphical view]
SUPFAMSSF56219. SSF56219. 1 hit.
PROSITEPS00919. DNASE_I_1. 1 hit.
PS00918. DNASE_I_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiDNASE1L2.
GenomeRNAi1775.
NextBio7227.
PROQ92874.
SOURCESearch...

Entry information

Entry nameDNSL2_HUMAN
AccessionPrimary (citable) accession number: Q92874
Secondary accession number(s): E9PBY4, Q6JVM2, Q6JVM3
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 1, 1997
Last modified: April 16, 2014
This is version 121 of the entry and version 1 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 chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM