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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei152NAD1 Publication1
Binding sitei182NAD1 Publication1
Sitei193Nicotinamide-stacking aromate1 Publication1
Binding sitei254NAD; may stabilize a reaction intermediate1 Publication1

GO - Molecular functioni

  • kinase binding Source: UniProtKB
  • NAD+ ADP-ribosyltransferase activity Source: UniProtKB
  • protein serine/threonine kinase activator activity Source: UniProtKB

GO - Biological processi

  • activation of signaling protein activity involved in unfolded protein response Source: UniProtKB
  • cellular response to leukemia inhibitory factor Source: Ensembl
  • endoplasmic reticulum unfolded protein response Source: UniProtKB
  • NAD biosynthesis via nicotinamide riboside salvage pathway Source: Reactome
  • negative regulation of cell death Source: UniProtKB
  • positive regulation of protein serine/threonine kinase activity Source: UniProtKB
  • protein ADP-ribosylation Source: UniProtKB
  • protein auto-ADP-ribosylation Source: UniProtKB

Keywordsi

Molecular functionGlycosyltransferase, Transferase
Biological processUnfolded protein response
LigandNAD

Enzyme and pathway databases

BRENDAi2.4.2.30. 2681.
2.4.2.31. 2681.
ReactomeiR-HSA-197264. Nicotinamide salvaging.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 15

Organism-specific databases

EuPathDBiHostDB:ENSG00000138617.14.
HGNCiHGNC:26040. PARP16.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 287CytoplasmicSequence analysisAdd BLAST287
Transmembranei288 – 308HelicalSequence analysisAdd BLAST21
Topological domaini309 – 322LumenalSequence analysisAdd BLAST14

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi152H → A: Loss of ADP-ribosyltransferase activity; when associated with A-254. 1 Publication1
Mutagenesisi152H → Q: ADP-ribosyltransferase activity is only 6% of wild-type; when associated with A-182. 1 Publication1
Mutagenesisi182Y → A: ADP-ribosyltransferase activity is only 6% of wild-type; when associated with Q-152. 1 Publication1
Mutagenesisi254Y → A: Loss of ADP-ribosyltransferase activity; when associated with H-152. 1 Publication1

Organism-specific databases

OpenTargetsiENSG00000138617.
PharmGKBiPA134984504.

Polymorphism and mutation databases

BioMutaiPARP16.
DMDMi116248565.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002524371 – 322Mono [ADP-ribose] polymerase PARP16Add BLAST322

Post-translational modificationi

Auto-ADP-ribosylated.2 Publications

Keywords - PTMi

ADP-ribosylation

Proteomic databases

EPDiQ8N5Y8.
MaxQBiQ8N5Y8.
PaxDbiQ8N5Y8.
PeptideAtlasiQ8N5Y8.
PRIDEiQ8N5Y8.

PTM databases

iPTMnetiQ8N5Y8.
PhosphoSitePlusiQ8N5Y8.

Expressioni

Gene expression databases

BgeeiENSG00000138617.
CleanExiHS_PARP16.
ExpressionAtlasiQ8N5Y8. baseline and differential.
GenevisibleiQ8N5Y8. HS.

Organism-specific databases

HPAiHPA017081.

Interactioni

Subunit structurei

Interacts with KPNB1.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
FLJ13057Q53SE73EBI-10266912,EBI-10172181

GO - Molecular functioni

  • kinase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi120294. 27 interactors.
IntActiQ8N5Y8. 9 interactors.
STRINGi9606.ENSP00000261888.

Structurei

Secondary structure

1322
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi6 – 15Combined sources10
Helixi17 – 32Combined sources16
Helixi36 – 39Combined sources4
Helixi45 – 47Combined sources3
Beta strandi48 – 51Combined sources4
Helixi55 – 63Combined sources9
Helixi68 – 72Combined sources5
Helixi80 – 89Combined sources10
Beta strandi93 – 99Combined sources7
Helixi103 – 111Combined sources9
Beta strandi123 – 130Combined sources8
Helixi134 – 142Combined sources9
Beta strandi147 – 153Combined sources7
Helixi156 – 158Combined sources3
Helixi159 – 165Combined sources7
Beta strandi176 – 178Combined sources3
Beta strandi181 – 185Combined sources5
Helixi187 – 191Combined sources5
Beta strandi207 – 218Combined sources12
Beta strandi255 – 257Combined sources3
Helixi260 – 262Combined sources3
Beta strandi263 – 272Combined sources10

3D structure databases

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

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini5 – 91PARP alpha-helicalAdd BLAST87
Domaini94 – 279PARP catalyticPROSITE-ProRule annotationAdd BLAST186

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi297 – 303Poly-Leu7

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

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IF6E. Eukaryota.
ENOG410ZP73. LUCA.
GeneTreeiENSGT00390000014077.
HOGENOMiHOG000253948.
HOVERGENiHBG058859.
InParanoidiQ8N5Y8.
KOiK00774.
OMAiLHNGLHC.
OrthoDBiEOG091G0E9B.
PhylomeDBiQ8N5Y8.
TreeFamiTF323413.

Family and domain databases

InterProiView protein in InterPro
IPR012317. Poly(ADP-ribose)pol_cat_dom.
PfamiView protein in Pfam
PF00644. PARP. 1 hit.
PROSITEiView protein in PROSITE
PS51059. PARP_CATALYTIC. 1 hit.

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)DescriptionActionsGraphical viewLength
Natural variantiVAR_027864280S → P1 PublicationCorresponds to variant dbSNP:rs17852901Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_02097359 – 173Missing in isoform 2. 1 PublicationAdd BLAST115
Alternative sequenceiVSP_020974277K → KS in isoform 3. 1 Publication1

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]
CCDS81897.1. [Q8N5Y8-2]
RefSeqiNP_001303872.1. NM_001316943.1. [Q8N5Y8-1]
NP_001303873.1. NM_001316944.1. [Q8N5Y8-2]
NP_060321.3. NM_017851.5. [Q8N5Y8-3]
UniGeneiHs.30634.

Genome annotation databases

EnsembliENST00000261888; ENSP00000261888; ENSG00000138617. [Q8N5Y8-3]
ENST00000444347; ENSP00000396118; ENSG00000138617. [Q8N5Y8-2]
GeneIDi54956.
KEGGihsa:54956.
UCSCiuc002aop.4. human. [Q8N5Y8-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Similar proteinsi

Entry informationi

Entry nameiPAR16_HUMAN
AccessioniPrimary (citable) accession number: Q8N5Y8
Secondary accession number(s): Q6PK64, Q9NX03
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 17, 2006
Last sequence update: October 17, 2006
Last modified: September 27, 2017
This is version 118 of the entry and version 2 of the sequence. See 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