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Q8N5Y8

- PAR16_HUMAN

UniProt

Q8N5Y8 - PAR16_HUMAN

Protein

Mono [ADP-ribose] polymerase PARP16

Gene

PARP16

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 93 (01 Oct 2014)
      Sequence version 2 (17 Oct 2006)
      Previous versions | rss
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    Functioni

    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.2 Publications

    Catalytic activityi

    NAD+ + protein-L-arginine = nicotinamide + N(omega)-(ADP-D-ribosyl)-protein-L-arginine.1 Publication

    Sites

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

    GO - Molecular functioni

    1. kinase binding Source: UniProt
    2. NAD(P)+-protein-arginine ADP-ribosyltransferase activity Source: UniProtKB-EC
    3. NAD+ ADP-ribosyltransferase activity Source: UniProt
    4. protein binding Source: UniProt
    5. protein serine/threonine kinase activator activity Source: UniProt

    GO - Biological processi

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

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Keywords - Biological processi

    Unfolded protein response

    Keywords - Ligandi

    NAD

    Enzyme and pathway databases

    BRENDAi2.4.2.30. 2681.

    Names & Taxonomyi

    Protein namesi
    Recommended 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 namesi
    Name:PARP16
    Synonyms:C15orf30
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 15

    Organism-specific databases

    HGNCiHGNC:26040. PARP16.

    Subcellular locationi

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    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

    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.

    Keywords - PTMi

    ADP-ribosylation

    Proteomic databases

    MaxQBiQ8N5Y8.
    PaxDbiQ8N5Y8.
    PRIDEiQ8N5Y8.

    PTM databases

    PhosphoSiteiQ8N5Y8.

    Expressioni

    Gene expression databases

    BgeeiQ8N5Y8.
    CleanExiHS_PARP16.
    GenevestigatoriQ8N5Y8.

    Organism-specific databases

    HPAiHPA017081.

    Interactioni

    Subunit structurei

    Interacts with KPNB1.2 Publications

    Protein-protein interaction databases

    BioGridi120294. 4 interactions.
    STRINGi9606.ENSP00000261888.

    Structurei

    Secondary structure

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

    3D structure databases

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

    Topological domain

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

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei288 – 30821HelicalSequence AnalysisAdd
    BLAST

    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.
    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. Align

    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

    MQPSGWAAAR EAAGRDMLAA DLRCSLFASA LQSYKRDSVL RPFPASYARG    50
    DCKDFEALLA DASKLPNLKE LLQSSGDNHK RAWDLVSWIL SSKVLTIHSA 100
    GKAEFEKIQK LTGAPHTPVP APDFLFEIEY FDPANAKFYE TKGERDLIYA 150
    FHGSRLENFH SIIHNGLHCH LNKTSLFGEG TYLTSDLSLA LIYSPHGHGW 200
    QHSLLGPILS CVAVCEVIDH PDVKCQTKKK DSKEIDRRRA RIKHSEGGDI 250
    PPKYFVVTNN QLLRVKYLLV YSQKPPKRAS SQLSWFSSHW FTVMISLYLL 300
    LLLIVSVINS SAFQHFWNRA KR 322
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK000516 mRNA. Translation: BAA91222.1 .
    BC006389 mRNA. Translation: AAH06389.1 .
    BC031074 mRNA. Translation: AAH31074.1 .
    CCDSi CCDS10204.1. [Q8N5Y8-3 ]
    RefSeqi NP_060321.3. NM_017851.4. [Q8N5Y8-3 ]
    XP_005254573.1. XM_005254516.2. [Q8N5Y8-1 ]
    UniGenei Hs.30634.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4F0D X-ray 2.70 A/B 5-279 [» ]
    ProteinModelPortali Q8N5Y8.
    SMRi Q8N5Y8. Positions 5-273.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 120294. 4 interactions.
    STRINGi 9606.ENSP00000261888.

    PTM databases

    PhosphoSitei Q8N5Y8.

    Polymorphism databases

    DMDMi 116248565.

    Proteomic databases

    MaxQBi Q8N5Y8.
    PaxDbi Q8N5Y8.
    PRIDEi Q8N5Y8.

    Protocols and materials databases

    DNASUi 54956.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000261888 ; ENSP00000261888 ; ENSG00000138617 . [Q8N5Y8-3 ]
    ENST00000444347 ; ENSP00000396118 ; ENSG00000138617 . [Q8N5Y8-2 ]
    GeneIDi 54956.
    KEGGi hsa:54956.
    UCSCi uc002aoo.3. human. [Q8N5Y8-1 ]
    uc002aop.3. human. [Q8N5Y8-2 ]
    uc002aoq.3. human. [Q8N5Y8-3 ]

    Organism-specific databases

    CTDi 54956.
    GeneCardsi GC15M065550.
    HGNCi HGNC:26040. PARP16.
    HPAi HPA017081.
    neXtProti NX_Q8N5Y8.
    PharmGKBi PA134984504.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG46092.
    HOGENOMi HOG000253948.
    HOVERGENi HBG058859.
    InParanoidi Q8N5Y8.
    KOi K00774.
    OMAi FHSILHN.
    PhylomeDBi Q8N5Y8.
    TreeFami TF323413.

    Enzyme and pathway databases

    BRENDAi 2.4.2.30. 2681.

    Miscellaneous databases

    GenomeRNAii 54956.
    NextBioi 58144.
    PROi Q8N5Y8.

    Gene expression databases

    Bgeei Q8N5Y8.
    CleanExi HS_PARP16.
    Genevestigatori Q8N5Y8.

    Family and domain databases

    Gene3Di 3.90.228.10. 1 hit.
    InterProi IPR012317. Poly(ADP-ribose)pol_cat_dom.
    [Graphical view ]
    Pfami PF00644. PARP. 1 hit.
    [Graphical view ]
    PROSITEi PS51059. PARP_CATALYTIC. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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(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.

    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: October 1, 2014
    This is version 93 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