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Q8N5Y8 (PAR16_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 89. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Mono [ADP-ribose] polymerase PARP16

EC=2.4.2.31
Alternative name(s):
ADP-ribosyltransferase diphtheria toxin-like 15
Short name=ARTD15
Poly [ADP-ribose] polymerase 16
Short name=PARP-16
Gene names
Name:PARP16
Synonyms:C15orf30
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length322 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Mono-ADP-ribosyltransferase targeting the karyopherin KPNB1. Plays a role in unfolded protein response (UPR), by ADP-ribosylating and activating EIF2AK3 and ERN1, two important UPR effectors. Ref.4 Ref.5

Catalytic activity

NAD+ + protein-L-arginine = nicotinamide + N(omega)-(ADP-D-ribosyl)-protein-L-arginine. Ref.5

Subunit structure

Interacts with KPNB1. Ref.5

Subcellular location

Nucleus membrane; Single-pass membrane protein. Endoplasmic reticulum membrane; Single-pass membrane protein Ref.4 Ref.5.

Domain

The N-terminal PARP alpha-helical domain is regulatory, it packs against the catalytic domain, and may relay effector-binding event to the NAD-binding site. Ref.6

Post-translational modification

ADP-ribosylated (-auto).

Sequence similarities

Contains 1 PARP alpha-helical domain.

Contains 1 PARP catalytic domain.

Ontologies

Keywords
   Biological processUnfolded protein response
   Cellular componentEndoplasmic reticulum
Membrane
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainTransmembrane
Transmembrane helix
   LigandNAD
   Molecular functionGlycosyltransferase
Transferase
   PTMADP-ribosylation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactivation of signaling protein activity involved in unfolded protein response

Inferred from mutant phenotype Ref.4. Source: UniProt

endoplasmic reticulum unfolded protein response

Inferred from mutant phenotype Ref.4. Source: UniProt

negative regulation of cell death

Inferred from mutant phenotype Ref.4. Source: UniProt

positive regulation of protein serine/threonine kinase activity

Inferred from mutant phenotype Ref.4. Source: UniProt

protein ADP-ribosylation

Inferred from mutant phenotype Ref.5Ref.4. Source: UniProt

protein auto-ADP-ribosylation

Inferred from mutant phenotype Ref.5Ref.4. Source: UniProt

   Cellular_componentendoplasmic reticulum

Inferred from mutant phenotype Ref.4. Source: UniProt

endoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

endoplasmic reticulum tubular network

Inferred from mutant phenotype Ref.5. Source: UniProt

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

nuclear envelope

Inferred from direct assay Ref.5. Source: UniProt

nuclear membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionNAD(P)+-protein-arginine ADP-ribosyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

NAD+ ADP-ribosyltransferase activity

Inferred from mutant phenotype Ref.5Ref.4. Source: UniProt

kinase binding

Inferred from physical interaction Ref.4. Source: UniProt

protein serine/threonine kinase activator activity

Inferred from mutant phenotype Ref.4. Source: UniProt

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8N5Y8-1)

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: Q8N5Y8-2)

The sequence of this isoform differs from the canonical sequence as follows:
     59-173: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q8N5Y8-3)

The sequence of this isoform differs from the canonical sequence as follows:
     277-277: K → KS
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 322322Mono [ADP-ribose] polymerase PARP16
PRO_0000252437

Regions

Topological domain1 – 287287Cytoplasmic Potential
Transmembrane288 – 30821Helical; Potential
Topological domain309 – 32214Lumenal Potential
Domain5 – 9187PARP alpha-helical
Domain94 – 279186PARP catalytic
Compositional bias297 – 3037Poly-Leu

Sites

Binding site1521NAD
Binding site1821NAD
Binding site2541NAD; may stabilize a reaction intermediate
Site1931Nicotinamide-stacking aromate

Natural variations

Alternative sequence59 – 173115Missing in isoform 2.
VSP_020973
Alternative sequence2771K → KS in isoform 3.
VSP_020974
Natural variant2801S → P. Ref.2
Corresponds to variant rs17852901 [ dbSNP | Ensembl ].
VAR_027864

Experimental info

Mutagenesis1521H → Q: ADP-ribosyltransferase activity is only 6% of wild-type; when associated with A-182. Ref.4
Mutagenesis1821Y → A: ADP-ribosyltransferase activity is only 6% of wild-type; when associated with Q-152. Ref.4

Secondary structure

.......................................... 322
Helix Strand Turn

Details...

Sequences

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

Last modified October 17, 2006. Version 2.
Checksum: DA1C99E8A1305982

FASTA32236,383
        10         20         30         40         50         60 
MQPSGWAAAR EAAGRDMLAA DLRCSLFASA LQSYKRDSVL RPFPASYARG DCKDFEALLA 

        70         80         90        100        110        120 
DASKLPNLKE LLQSSGDNHK RAWDLVSWIL SSKVLTIHSA GKAEFEKIQK LTGAPHTPVP 

       130        140        150        160        170        180 
APDFLFEIEY FDPANAKFYE TKGERDLIYA FHGSRLENFH SIIHNGLHCH LNKTSLFGEG 

       190        200        210        220        230        240 
TYLTSDLSLA LIYSPHGHGW QHSLLGPILS CVAVCEVIDH PDVKCQTKKK DSKEIDRRRA 

       250        260        270        280        290        300 
RIKHSEGGDI PPKYFVVTNN QLLRVKYLLV YSQKPPKRAS SQLSWFSSHW FTVMISLYLL 

       310        320 
LLLIVSVINS SAFQHFWNRA KR 

« Hide

Isoform 2 [UniParc].

Checksum: 5D9F59FCAFBBBA13
Show »

FASTA20723,378
Isoform 3 [UniParc].

Checksum: 3F3ED063887CB0EE
Show »

FASTA32336,470

References

« Hide 'large scale' references
[1]"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 2).
Tissue: Carcinoma.
[2]"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] (ISOFORMS 1 AND 3), VARIANT PRO-280.
Tissue: Brain.
[3]"Toward a unified nomenclature for mammalian ADP-ribosyltransferases."
Hottiger M.O., Hassa P.O., Luscher B., Schuler H., Koch-Nolte F.
Trends Biochem. Sci. 35:208-219(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NOMENCLATURE.
[4]"PARP16 is a tail-anchored endoplasmic reticulum protein required for the PERK-and IRE1alpha-mediated unfolded protein response."
Jwa M., Chang P.
Nat. Cell Biol. 14:1223-1230(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF HIS-152 AND TYR-182.
[5]"PARP16/ARTD15 is a novel endoplasmic-reticulum-associated mono-ADP-ribosyltransferase that interacts with, and modifies karyopherin-beta1."
Di Paola S., Micaroni M., Di Tullio G., Buccione R., Di Girolamo M.
PLoS ONE 7:E37352-E37352(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, INTERACTION WITH KPNB1, CATALYTIC ACTIVITY.
[6]"Crystal structure of human ADP-ribose transferase ARTD15/PARP16 reveals a novel putative regulatory domain."
Karlberg T., Thorsell A.G., Kallas A., Schuler H.
J. Biol. Chem. 287:24077-24081(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 5-279 IN COMPLEX WITH NAD ANALOG, AUTO-ADP-RIBOSYLATION, DOMAIN PARP ALPHA-HELICAL, NAD-BINDING SITES.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK000516 mRNA. Translation: BAA91222.1.
BC006389 mRNA. Translation: AAH06389.1.
BC031074 mRNA. Translation: AAH31074.1.
RefSeqNP_060321.3. NM_017851.4.
XP_005254573.1. XM_005254516.2.
UniGeneHs.30634.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4F0DX-ray2.70A/B5-279[»]
ProteinModelPortalQ8N5Y8.
SMRQ8N5Y8. Positions 5-273.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid120294. 4 interactions.
STRING9606.ENSP00000261888.

PTM databases

PhosphoSiteQ8N5Y8.

Polymorphism databases

DMDM116248565.

Proteomic databases

PaxDbQ8N5Y8.
PRIDEQ8N5Y8.

Protocols and materials databases

DNASU54956.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000261888; ENSP00000261888; ENSG00000138617. [Q8N5Y8-3]
ENST00000444347; ENSP00000396118; ENSG00000138617. [Q8N5Y8-2]
GeneID54956.
KEGGhsa:54956.
UCSCuc002aoo.3. human. [Q8N5Y8-1]
uc002aop.3. human. [Q8N5Y8-2]
uc002aoq.3. human. [Q8N5Y8-3]

Organism-specific databases

CTD54956.
GeneCardsGC15M065550.
HGNCHGNC:26040. PARP16.
HPAHPA017081.
neXtProtNX_Q8N5Y8.
PharmGKBPA134984504.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG46092.
HOGENOMHOG000253948.
HOVERGENHBG058859.
InParanoidQ8N5Y8.
KOK00774.
OMAFHSILHN.
PhylomeDBQ8N5Y8.
TreeFamTF323413.

Enzyme and pathway databases

BRENDA2.4.2.30. 2681.

Gene expression databases

BgeeQ8N5Y8.
CleanExHS_PARP16.
GenevestigatorQ8N5Y8.

Family and domain databases

Gene3D3.90.228.10. 1 hit.
InterProIPR012317. Poly(ADP-ribose)pol_cat_dom.
[Graphical view]
PfamPF00644. PARP. 1 hit.
[Graphical view]
PROSITEPS51059. PARP_CATALYTIC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi54956.
NextBio58144.
PROQ8N5Y8.

Entry information

Entry namePAR16_HUMAN
AccessionPrimary (citable) accession number: Q8N5Y8
Secondary accession number(s): Q6PK64, Q9NX03
Entry history
Integrated into UniProtKB/Swiss-Prot: October 17, 2006
Last sequence update: October 17, 2006
Last modified: April 16, 2014
This is version 89 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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 15

Human chromosome 15: entries, gene names and cross-references to MIM