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Protein

Mono [ADP-ribose] polymerase PARP16

Gene

PARP16

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

Functioni

Intracellular mono-ADP-ribosyltransferase that may play a role in different processes through the mono-ADP-ribosylation of proteins involved in those processes (PubMed:23103912, PubMed:22701565). May play a role in the unfolded protein response (UPR), by ADP-ribosylating and activating EIF2AK3 and ERN1, two important UPR effectors (PubMed:23103912). May also mediate mono-ADP-ribosylation of karyopherin KPNB1 a nuclear import factor (PubMed:22701565). May not modify proteins on arginine, cysteine or glutamate residues compared to other mono-ADP-ribosyltransferases (PubMed:22701565).2 Publications

Catalytic activityi

NAD+ + (ADP-D-ribosyl)(n)-acceptor = nicotinamide + (ADP-D-ribosyl)(n+1)-acceptor.1 Publication

Kineticsi

  1. KM=290 µM for NAD (at 37 degrees Celsius)1 Publication

Vmax=0.7 pmol/h/µg enzyme (at 37 degrees Celsius)1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei152 – 1521NAD
Binding sitei182 – 1821NAD
Sitei193 – 1931Nicotinamide-stacking aromate1 Publication
Binding sitei254 – 2541NAD; may stabilize a reaction intermediate

GO - Molecular functioni

  1. kinase binding Source: UniProtKB
  2. NAD+ ADP-ribosyltransferase activity Source: UniProtKB
  3. protein serine/threonine kinase activator activity Source: UniProtKB

GO - Biological processi

  1. activation of signaling protein activity involved in unfolded protein response Source: UniProtKB
  2. endoplasmic reticulum unfolded protein response Source: UniProtKB
  3. negative regulation of cell death Source: UniProtKB
  4. positive regulation of protein serine/threonine kinase activity Source: UniProtKB
  5. protein ADP-ribosylation Source: UniProtKB
  6. protein auto-ADP-ribosylation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Unfolded protein response

Keywords - Ligandi

NAD

Enzyme and pathway databases

BRENDAi2.4.2.30. 2681.
2.4.2.31. 2681.

Names & Taxonomyi

Protein namesi
Recommended name:
Mono [ADP-ribose] polymerase PARP16Curated (EC:2.4.2.301 Publication)
Alternative name(s):
ADP-ribosyltransferase diphtheria toxin-like 151 Publication
Poly [ADP-ribose] polymerase 16
Short name:
PARP-16
Gene namesi
Name:PARP161 PublicationImported
Synonyms:ARTD151 Publication, C15orf30Imported
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 15

Organism-specific databases

HGNCiHGNC:26040. PARP16.

Subcellular locationi

Endoplasmic reticulum membrane; Single-pass type IV membrane protein 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 287287CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei288 – 30821HelicalSequence AnalysisAdd
BLAST
Topological domaini309 – 32214LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum Source: UniProtKB
  2. endoplasmic reticulum membrane Source: UniProtKB-SubCell
  3. endoplasmic reticulum tubular network Source: UniProtKB
  4. integral component of membrane Source: UniProtKB-KW
  5. membrane Source: UniProtKB
  6. nuclear envelope Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi152 – 1521H → A: Loss of ADP-ribosyltransferase activity; when associated with A-254. 1 Publication
Mutagenesisi152 – 1521H → Q: ADP-ribosyltransferase activity is only 6% of wild-type; when associated with A-182. 1 Publication
Mutagenesisi182 – 1821Y → A: ADP-ribosyltransferase activity is only 6% of wild-type; when associated with Q-152. 1 Publication
Mutagenesisi254 – 2541Y → A: Loss of ADP-ribosyltransferase activity; when associated with H-152. 1 Publication

Organism-specific databases

PharmGKBiPA134984504.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 322322Mono [ADP-ribose] polymerase PARP16PRO_0000252437Add
BLAST

Post-translational modificationi

Auto-ADP-ribosylated.2 Publications

Keywords - PTMi

ADP-ribosylation

Proteomic databases

MaxQBiQ8N5Y8.
PaxDbiQ8N5Y8.
PRIDEiQ8N5Y8.

PTM databases

PhosphoSiteiQ8N5Y8.

Expressioni

Gene expression databases

BgeeiQ8N5Y8.
CleanExiHS_PARP16.
ExpressionAtlasiQ8N5Y8. baseline and differential.
GenevestigatoriQ8N5Y8.

Organism-specific databases

HPAiHPA017081.

Interactioni

Subunit structurei

Interacts with KPNB1.2 Publications

Protein-protein interaction databases

BioGridi120294. 21 interactions.
STRINGi9606.ENSP00000261888.

Structurei

Secondary structure

1
322
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 1510Combined sources
Helixi17 – 3216Combined sources
Helixi36 – 394Combined sources
Helixi45 – 473Combined sources
Beta strandi48 – 514Combined sources
Helixi55 – 639Combined sources
Helixi68 – 725Combined sources
Helixi80 – 8910Combined sources
Beta strandi93 – 997Combined sources
Helixi103 – 1119Combined sources
Beta strandi123 – 1308Combined sources
Helixi134 – 1429Combined sources
Beta strandi147 – 1537Combined sources
Helixi156 – 1583Combined sources
Helixi159 – 1657Combined sources
Beta strandi176 – 1783Combined sources
Beta strandi181 – 1855Combined sources
Helixi187 – 1915Combined sources
Beta strandi207 – 21812Combined sources
Beta strandi255 – 2573Combined sources
Helixi260 – 2623Combined sources
Beta strandi263 – 27210Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4F0DX-ray2.70A/B5-279[»]
ProteinModelPortaliQ8N5Y8.
SMRiQ8N5Y8. Positions 5-273.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini5 – 9187PARP alpha-helicalAdd
BLAST
Domaini94 – 279186PARP catalyticPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi297 – 3037Poly-Leu

Domaini

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.1 Publication

Sequence similaritiesi

Contains 1 PARP alpha-helical domain.Curated
Contains 1 PARP catalytic domain.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG46092.
GeneTreeiENSGT00390000014077.
HOGENOMiHOG000253948.
HOVERGENiHBG058859.
InParanoidiQ8N5Y8.
KOiK00774.
OMAiFHSILHN.
PhylomeDBiQ8N5Y8.
TreeFamiTF323413.

Family and domain databases

Gene3Di3.90.228.10. 1 hit.
InterProiIPR012317. Poly(ADP-ribose)pol_cat_dom.
[Graphical view]
PfamiPF00644. PARP. 1 hit.
[Graphical view]
PROSITEiPS51059. PARP_CATALYTIC. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8N5Y8-1) [UniParc]FASTAAdd to basket

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
MQPSGWAAAR EAAGRDMLAA DLRCSLFASA LQSYKRDSVL RPFPASYARG
60 70 80 90 100
DCKDFEALLA DASKLPNLKE LLQSSGDNHK RAWDLVSWIL SSKVLTIHSA
110 120 130 140 150
GKAEFEKIQK LTGAPHTPVP APDFLFEIEY FDPANAKFYE TKGERDLIYA
160 170 180 190 200
FHGSRLENFH SIIHNGLHCH LNKTSLFGEG TYLTSDLSLA LIYSPHGHGW
210 220 230 240 250
QHSLLGPILS CVAVCEVIDH PDVKCQTKKK DSKEIDRRRA RIKHSEGGDI
260 270 280 290 300
PPKYFVVTNN QLLRVKYLLV YSQKPPKRAS SQLSWFSSHW FTVMISLYLL
310 320
LLLIVSVINS SAFQHFWNRA KR
Length:322
Mass (Da):36,383
Last modified:October 17, 2006 - v2
Checksum:iDA1C99E8A1305982
GO
Isoform 2 (identifier: Q8N5Y8-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     59-173: Missing.

Note: No experimental confirmation available.

Show »
Length:207
Mass (Da):23,378
Checksum:i5D9F59FCAFBBBA13
GO
Isoform 3 (identifier: Q8N5Y8-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     277-277: K → KS

Note: No experimental confirmation available.

Show »
Length:323
Mass (Da):36,470
Checksum:i3F3ED063887CB0EE
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti280 – 2801S → P.1 Publication
Corresponds to variant rs17852901 [ dbSNP | Ensembl ].
VAR_027864

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei59 – 173115Missing in isoform 2. 1 PublicationVSP_020973Add
BLAST
Alternative sequencei277 – 2771K → KS in isoform 3. 1 PublicationVSP_020974

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK000516 mRNA. Translation: BAA91222.1.
BC006389 mRNA. Translation: AAH06389.1.
BC031074 mRNA. Translation: AAH31074.1.
CCDSiCCDS10204.1. [Q8N5Y8-3]
RefSeqiNP_060321.3. NM_017851.4. [Q8N5Y8-3]
XP_005254573.1. XM_005254516.2. [Q8N5Y8-1]
UniGeneiHs.30634.

Genome annotation databases

EnsembliENST00000261888; ENSP00000261888; ENSG00000138617. [Q8N5Y8-3]
ENST00000444347; ENSP00000396118; ENSG00000138617. [Q8N5Y8-2]
GeneIDi54956.
KEGGihsa:54956.
UCSCiuc002aoo.3. human. [Q8N5Y8-1]
uc002aop.3. human. [Q8N5Y8-2]
uc002aoq.3. human. [Q8N5Y8-3]

Polymorphism databases

DMDMi116248565.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK000516 mRNA. Translation: BAA91222.1.
BC006389 mRNA. Translation: AAH06389.1.
BC031074 mRNA. Translation: AAH31074.1.
CCDSiCCDS10204.1. [Q8N5Y8-3]
RefSeqiNP_060321.3. NM_017851.4. [Q8N5Y8-3]
XP_005254573.1. XM_005254516.2. [Q8N5Y8-1]
UniGeneiHs.30634.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4F0DX-ray2.70A/B5-279[»]
ProteinModelPortaliQ8N5Y8.
SMRiQ8N5Y8. Positions 5-273.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120294. 21 interactions.
STRINGi9606.ENSP00000261888.

PTM databases

PhosphoSiteiQ8N5Y8.

Polymorphism databases

DMDMi116248565.

Proteomic databases

MaxQBiQ8N5Y8.
PaxDbiQ8N5Y8.
PRIDEiQ8N5Y8.

Protocols and materials databases

DNASUi54956.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000261888; ENSP00000261888; ENSG00000138617. [Q8N5Y8-3]
ENST00000444347; ENSP00000396118; ENSG00000138617. [Q8N5Y8-2]
GeneIDi54956.
KEGGihsa:54956.
UCSCiuc002aoo.3. human. [Q8N5Y8-1]
uc002aop.3. human. [Q8N5Y8-2]
uc002aoq.3. human. [Q8N5Y8-3]

Organism-specific databases

CTDi54956.
GeneCardsiGC15M065550.
HGNCiHGNC:26040. PARP16.
HPAiHPA017081.
neXtProtiNX_Q8N5Y8.
PharmGKBiPA134984504.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG46092.
GeneTreeiENSGT00390000014077.
HOGENOMiHOG000253948.
HOVERGENiHBG058859.
InParanoidiQ8N5Y8.
KOiK00774.
OMAiFHSILHN.
PhylomeDBiQ8N5Y8.
TreeFamiTF323413.

Enzyme and pathway databases

BRENDAi2.4.2.30. 2681.
2.4.2.31. 2681.

Miscellaneous databases

GenomeRNAii54956.
NextBioi58144.
PROiQ8N5Y8.

Gene expression databases

BgeeiQ8N5Y8.
CleanExiHS_PARP16.
ExpressionAtlasiQ8N5Y8. baseline and differential.
GenevestigatoriQ8N5Y8.

Family and domain databases

Gene3Di3.90.228.10. 1 hit.
InterProiIPR012317. Poly(ADP-ribose)pol_cat_dom.
[Graphical view]
PfamiPF00644. PARP. 1 hit.
[Graphical view]
PROSITEiPS51059. PARP_CATALYTIC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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(2003) [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(2003) [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(2009) [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(2011) [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(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, INTERACTION WITH KPNB1, CATALYTIC ACTIVITY, MUTAGENESIS OF HIS-152 AND TYR-254, BIOPHYSICOCHEMICAL PROPERTIES, AUTO-ADP-RIBOSYLATION.
  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(2011) [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.

Entry informationi

Entry nameiPAR16_HUMAN
AccessioniPrimary (citable) accession number: Q8N5Y8
Secondary accession number(s): Q6PK64, Q9NX03
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 17, 2006
Last sequence update: October 17, 2006
Last modified: April 1, 2015
This is version 99 of the entry and version 2 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 15
    Human chromosome 15: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. 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.