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Protein

Mono [ADP-ribose] polymerase PARP16

Gene

Parp16

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript 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. May play a role in the unfolded protein response (UPR), by ADP-ribosylating and activating EIF2AK3 and ERN1, two important UPR effectors. May also mediate mono-ADP-ribosylation of karyopherin KPNB1 a nuclear import factor. May not modify proteins on arginine, cysteine or glutamate residues compared to other mono-ADP-ribosyltransferases.By similarity

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei152NADBy similarity1
Binding sitei182NADBy similarity1
Sitei193Nicotinamide-stacking aromateBy similarity1
Binding sitei254NAD; may stabilize a reaction intermediateBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Unfolded protein response

Keywords - Ligandi

NAD

Names & Taxonomyi

Protein namesi
Recommended name:
Mono [ADP-ribose] polymerase PARP16Curated (EC:2.4.2.30By similarity)
Alternative name(s):
ADP-ribosyltransferase diphtheria toxin-like 15
Poly [ADP-ribose] polymerase 16
Short name:
PARP-16
Gene namesi
Name:Parp16Imported
Synonyms:Artd15Imported
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi1306243. Parp16.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transmembranei285 – 305HelicalSequence analysisAdd BLAST21

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002524391 – 322Mono [ADP-ribose] polymerase PARP16Add BLAST322

Post-translational modificationi

Auto-ADP-ribosylated.By similarity

Keywords - PTMi

ADP-ribosylation

Proteomic databases

PaxDbiQ5U2Q4.
PRIDEiQ5U2Q4.

Expressioni

Gene expression databases

BgeeiENSRNOG00000029127.

Interactioni

Subunit structurei

Interacts with KPNB1.By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000043841.

Structurei

3D structure databases

ProteinModelPortaliQ5U2Q4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini5 – 91PARP alpha-helicalAdd BLAST87
Domaini77 – 280PARP catalyticPROSITE-ProRule annotationAdd BLAST204

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.By similarity

Sequence similaritiesi

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

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IF6E. Eukaryota.
ENOG410ZP73. LUCA.
HOVERGENiHBG058859.
InParanoidiQ5U2Q4.
KOiK00774.

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]

Sequencei

Sequence statusi: Complete.

Q5U2Q4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQLSNRAAAR ESVSRDVLAA DLRCSLFASA LQSYKRDSVL RPFPASYARH
60 70 80 90 100
DCKDFEALLA DTGRLPNLKE LLQSSRDTDK QTWDLVSWIL SSKILTIHSA
110 120 130 140 150
EKAEFEKIQQ LTGAPHTPVP IPDFLFEIEY FDPANARFYE TKGGRDLIYA
160 170 180 190 200
FHGSRLENFH SIIHNGLHCH LNKTSLFGEG TYLTSDLSLA LIYSPHGRGW
210 220 230 240 250
QHSLLGQTLS CVAVCEVIDH PDVKCQTKKK DSKEIDRSRA RIKHSEGGDV
260 270 280 290 300
PPKYFVVTNN QLLRVKYLLV YSQKQPKRAS SQLSWLCSHW FMVAMSLYLL
310 320
LLLIVSVTNS SAFQHFWNRL KR
Length:322
Mass (Da):36,712
Last modified:December 7, 2004 - v1
Checksum:i9D45121DB8D093CF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC085908 mRNA. Translation: AAH85908.1.
RefSeqiNP_001014115.1. NM_001014093.1.
XP_006243320.1. XM_006243258.3.
UniGeneiRn.23423.

Genome annotation databases

GeneIDi315760.
KEGGirno:315760.
UCSCiRGD:1306243. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC085908 mRNA. Translation: AAH85908.1.
RefSeqiNP_001014115.1. NM_001014093.1.
XP_006243320.1. XM_006243258.3.
UniGeneiRn.23423.

3D structure databases

ProteinModelPortaliQ5U2Q4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000043841.

Proteomic databases

PaxDbiQ5U2Q4.
PRIDEiQ5U2Q4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi315760.
KEGGirno:315760.
UCSCiRGD:1306243. rat.

Organism-specific databases

CTDi54956.
RGDi1306243. Parp16.

Phylogenomic databases

eggNOGiENOG410IF6E. Eukaryota.
ENOG410ZP73. LUCA.
HOVERGENiHBG058859.
InParanoidiQ5U2Q4.
KOiK00774.

Miscellaneous databases

PROiQ5U2Q4.

Gene expression databases

BgeeiENSRNOG00000029127.

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...

Entry informationi

Entry nameiPAR16_RAT
AccessioniPrimary (citable) accession number: Q5U2Q4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 17, 2006
Last sequence update: December 7, 2004
Last modified: November 2, 2016
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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 one 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.