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Protein

Deoxyribonuclease-1-like 2

Gene

DNASE1L2

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

Functioni

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.1 Publication

Cofactori

Protein has several cofactor binding sites:
  • Mg2+1 Publication
  • Ca2+1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei99 – 991By similarity
Active sitei170 – 1701By similarity

GO - Molecular functioni

  1. calcium ion binding Source: ProtInc
  2. deoxyribonuclease activity Source: ProtInc
  3. DNA binding Source: ProtInc
  4. endodeoxyribonuclease activity Source: GO_Central
  5. endodeoxyribonuclease activity, producing 5'-phosphomonoesters Source: InterPro

GO - Biological processi

  1. corneocyte development Source: Ensembl
  2. DNA catabolic process, endonucleolytic Source: GO_Central
  3. DNA metabolic process Source: ProtInc
  4. hair follicle development Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Hydrolase, Nuclease

Keywords - Ligandi

Calcium, Magnesium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:DNASE1L2
Synonyms:DHP1, DNAS1L2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 16

Organism-specific databases

HGNCiHGNC:2958. DNASE1L2.

Subcellular locationi

Cytoplasm 1 Publication. Secreted Curated

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. extracellular region Source: UniProtKB-SubCell
  3. nucleus Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27429.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Sequence AnalysisAdd
BLAST
Chaini21 – 299279Deoxyribonuclease-1-like 2PRO_0000007286Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi209 ↔ 245Essential for enzymatic activityBy similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiQ92874.
PRIDEiQ92874.

Expressioni

Tissue specificityi

Preferentially expressed in the skin and up-regulated during keratinocytes differentiation. Highly abundant (at protein level) in the stratum granulosum.1 Publication

Inductioni

Up-regulated by inflammatory cytokines.1 Publication

Gene expression databases

BgeeiQ92874.
CleanExiHS_DNASE1L2.
ExpressionAtlasiQ92874. baseline and differential.
GenevestigatoriQ92874.

Organism-specific databases

HPAiHPA044714.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
ABL1P005191EBI-1751995,EBI-375543
FYNP062411EBI-1751995,EBI-515315

Protein-protein interaction databases

BioGridi108114. 7 interactions.
IntActiQ92874. 2 interactions.
MINTiMINT-4722563.
STRINGi9606.ENSP00000316938.

Structurei

3D structure databases

ProteinModelPortaliQ92874.
SMRiQ92874. Positions 22-296.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the DNase I family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG46375.
GeneTreeiENSGT00390000013146.
HOGENOMiHOG000059570.
HOVERGENiHBG051368.
InParanoidiQ92874.
KOiK11995.
OMAiYQYPDPE.
OrthoDBiEOG73V6KW.
PhylomeDBiQ92874.
TreeFamiTF329541.

Family and domain databases

Gene3Di3.60.10.10. 1 hit.
InterProiIPR018057. Deoxyribonuclease-1_AS.
IPR016202. DNase_I.
IPR005135. Endo/exonuclease/phosphatase.
[Graphical view]
PANTHERiPTHR11371. PTHR11371. 1 hit.
PfamiPF03372. Exo_endo_phos. 1 hit.
[Graphical view]
PIRSFiPIRSF000988. DNase_I_euk. 1 hit.
PRINTSiPR00130. DNASEI.
SMARTiSM00476. DNaseIc. 1 hit.
[Graphical view]
SUPFAMiSSF56219. SSF56219. 1 hit.
PROSITEiPS00919. DNASE_I_1. 1 hit.
PS00918. DNASE_I_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q92874-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MGGPRALLAA LWALEAAGTA ALRIGAFNIQ SFGDSKVSDP ACGSIIAKIL
60 70 80 90 100
AGYDLALVQE VRDPDLSAVS ALMEQINSVS EHEYSFVSSQ PLGRDQYKEM
110 120 130 140 150
YLFVYRKDAV SVVDTYLYPD PEDVFSREPF VVKFSAPGTG ERAPPLPSRR
160 170 180 190 200
ALTPPPLPAA AQNLVLIPLH AAPHQAVAEI DALYDVYLDV IDKWGTDDML
210 220 230 240 250
FLGDFNADCS YVRAQDWAAI RLRSSEVFKW LIPDSADTTV GNSDCAYDRI
260 270 280 290
VACGARLRRS LKPQSATVHD FQEEFGLDQT QALAISDHFP VEVTLKFHR
Length:299
Mass (Da):32,853
Last modified:February 1, 1997 - v1
Checksum:i1B66A5590D33D0A6
GO
Isoform 2 (identifier: Q92874-2) [UniParc]FASTAAdd to basket

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.

Show »
Length:278
Mass (Da):30,707
Checksum:i076B44856A08D0BE
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei140 – 16021Missing in isoform 2. 1 PublicationVSP_053879Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS42105.1. [Q92874-1]
RefSeqiNP_001288609.1. NM_001301680.1. [Q92874-1]
NP_001365.1. NM_001374.2. [Q92874-1]
XP_006720919.1. XM_006720856.1. [Q92874-1]
UniGeneiHs.103503.

Genome annotation databases

EnsembliENST00000320700; ENSP00000316938; ENSG00000167968. [Q92874-1]
ENST00000382437; ENSP00000371874; ENSG00000167968. [Q92874-2]
ENST00000564065; ENSP00000454562; ENSG00000167968. [Q92874-1]
ENST00000567494; ENSP00000455358; ENSG00000167968. [Q92874-1]
ENST00000613572; ENSP00000482627; ENSG00000167968. [Q92874-2]
GeneIDi1775.
KEGGihsa:1775.
UCSCiuc002cpn.3. human.
uc002cpo.3. human. [Q92874-1]

Polymorphism databases

DMDMi2494172.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS42105.1. [Q92874-1]
RefSeqiNP_001288609.1. NM_001301680.1. [Q92874-1]
NP_001365.1. NM_001374.2. [Q92874-1]
XP_006720919.1. XM_006720856.1. [Q92874-1]
UniGeneiHs.103503.

3D structure databases

ProteinModelPortaliQ92874.
SMRiQ92874. Positions 22-296.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108114. 7 interactions.
IntActiQ92874. 2 interactions.
MINTiMINT-4722563.
STRINGi9606.ENSP00000316938.

Polymorphism databases

DMDMi2494172.

Proteomic databases

PaxDbiQ92874.
PRIDEiQ92874.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000320700; ENSP00000316938; ENSG00000167968. [Q92874-1]
ENST00000382437; ENSP00000371874; ENSG00000167968. [Q92874-2]
ENST00000564065; ENSP00000454562; ENSG00000167968. [Q92874-1]
ENST00000567494; ENSP00000455358; ENSG00000167968. [Q92874-1]
ENST00000613572; ENSP00000482627; ENSG00000167968. [Q92874-2]
GeneIDi1775.
KEGGihsa:1775.
UCSCiuc002cpn.3. human.
uc002cpo.3. human. [Q92874-1]

Organism-specific databases

CTDi1775.
GeneCardsiGC16P002285.
H-InvDBHIX0038772.
HGNCiHGNC:2958. DNASE1L2.
HPAiHPA044714.
MIMi602622. gene.
neXtProtiNX_Q92874.
PharmGKBiPA27429.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG46375.
GeneTreeiENSGT00390000013146.
HOGENOMiHOG000059570.
HOVERGENiHBG051368.
InParanoidiQ92874.
KOiK11995.
OMAiYQYPDPE.
OrthoDBiEOG73V6KW.
PhylomeDBiQ92874.
TreeFamiTF329541.

Miscellaneous databases

GeneWikiiDNASE1L2.
GenomeRNAii1775.
NextBioi7227.
PROiQ92874.
SOURCEiSearch...

Gene expression databases

BgeeiQ92874.
CleanExiHS_DNASE1L2.
ExpressionAtlasiQ92874. baseline and differential.
GenevestigatoriQ92874.

Family and domain databases

Gene3Di3.60.10.10. 1 hit.
InterProiIPR018057. Deoxyribonuclease-1_AS.
IPR016202. DNase_I.
IPR005135. Endo/exonuclease/phosphatase.
[Graphical view]
PANTHERiPTHR11371. PTHR11371. 1 hit.
PfamiPF03372. Exo_endo_phos. 1 hit.
[Graphical view]
PIRSFiPIRSF000988. DNase_I_euk. 1 hit.
PRINTSiPR00130. DNASEI.
SMARTiSM00476. DNaseIc. 1 hit.
[Graphical view]
SUPFAMiSSF56219. SSF56219. 1 hit.
PROSITEiPS00919. DNASE_I_1. 1 hit.
PS00918. DNASE_I_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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. 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. Cited for: FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiDNSL2_HUMAN
AccessioniPrimary (citable) accession number: Q92874
Secondary accession number(s): E9PBY4, Q6JVM2, Q6JVM3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 1, 1997
Last modified: February 4, 2015
This is version 129 of the entry and version 1 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.