Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9NVV4

- PAPD1_HUMAN

UniProt

Q9NVV4 - PAPD1_HUMAN

Protein

Poly(A) RNA polymerase, mitochondrial

Gene

MTPAP

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 109 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Polymerase that creates the 3' poly(A) tail of mitochondrial transcripts. Can use all four nucleotides, but has higher activity with ATP and UTP (in vitro). Plays a role in replication-dependent histone mRNA degradation. May be involved in the terminal uridylation of mature histone mRNAs before their degradation is initiated. Might be responsible for the creation of some UAA stop codons which are not encoded in mtDNA.5 Publications

    Catalytic activityi

    ATP + RNA(n) = diphosphate + RNA(n+1).2 Publications

    Cofactori

    Magnesium or manganese.1 Publication

    Kineticsi

    1. KM=0.1 mM for ATP1 Publication
    2. KM=0.7 mM for UTP1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi243 – 2431Magnesium or manganese; catalyticBy similarity
    Metal bindingi245 – 2451Magnesium or manganese; catalyticBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi107 – 1093ATPSequence Analysis
    Nucleotide bindingi241 – 2422ATPSequence Analysis

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB
    2. identical protein binding Source: IntAct
    3. magnesium ion binding Source: UniProtKB
    4. manganese ion binding Source: UniProtKB
    5. poly(A) RNA binding Source: UniProtKB
    6. polynucleotide adenylyltransferase activity Source: UniProtKB
    7. protein binding Source: IntAct
    8. protein homodimerization activity Source: UniProtKB
    9. UTP binding Source: UniProtKB

    GO - Biological processi

    1. cell death Source: UniProtKB-KW
    2. histone mRNA catabolic process Source: UniProtKB
    3. mRNA polyadenylation Source: UniProtKB
    4. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Nucleotidyltransferase, Transferase

    Keywords - Biological processi

    mRNA processing, Transcription

    Keywords - Ligandi

    ATP-binding, Magnesium, Manganese, Metal-binding, Nucleotide-binding, RNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Poly(A) RNA polymerase, mitochondrial (EC:2.7.7.19)
    Short name:
    PAP
    Alternative name(s):
    PAP-associated domain-containing protein 1
    Polynucleotide adenylyltransferase
    Terminal uridylyltransferase 1
    Short name:
    TUTase 1
    mtPAP
    Gene namesi
    Name:MTPAP
    Synonyms:PAPD1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:25532. MTPAP.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. Golgi apparatus Source: HPA
    3. mitochondrion Source: HPA
    4. nucleus Source: HPA
    5. plasma membrane Source: HPA

    Keywords - Cellular componenti

    Cytoplasm, Mitochondrion

    Pathology & Biotechi

    Involvement in diseasei

    Spastic ataxia 4, autosomal recessive (SPAX4) [MIM:613672]: A slowly progressive neurodegenerative disease characterized by cerebellar ataxia, spastic paraparesis, dysarthria, and optic atrophy.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry. MTPAP mutations result in a defect of mitochondrial mRNA maturation. Affected individuals exhibit a drastic decrease in poly(A) tail length of mitochondrial mRNA transcripts, including COX1 and RNA14 (PubMed:20970105).1 Publication
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti478 – 4781N → D in SPAX4. 1 Publication
    VAR_064907

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi221 – 2222YF → AA: Reduces dimerization.
    Mutagenesisi230 – 2301F → A: Reduced enzyme activity. 1 Publication
    Mutagenesisi259 – 2613HKI → AAA: No effect on dimerization. Loss of dimerization and of enzyme activity; when associated with 294-AAAA-297.
    Mutagenesisi294 – 2974HFGP → AAGA: Reduced dimerization. Loss of dimerization and of enzyme activity; when associated with 259-AAA-261.
    Mutagenesisi312 – 3121L → A: Reduced enzyme activity. 1 Publication
    Mutagenesisi325 – 3251D → A: Loss of enzyme activity. 1 Publication
    Mutagenesisi378 – 3781F → A: Reduced enzyme activity. 1 Publication

    Keywords - Diseasei

    Disease mutation, Neurodegeneration

    Organism-specific databases

    MIMi613672. phenotype.
    Orphaneti254343. Autosomal recessive spastic ataxia - optic atrophy - dysarthria.
    PharmGKBiPA164723192.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 3737MitochondrionSequence AnalysisAdd
    BLAST
    Chaini38 – 582545Poly(A) RNA polymerase, mitochondrialPRO_0000250689Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei90 – 901N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ9NVV4.
    PaxDbiQ9NVV4.
    PRIDEiQ9NVV4.

    PTM databases

    PhosphoSiteiQ9NVV4.

    Expressioni

    Tissue specificityi

    Ubiquitous, with stronger expression in tissues with high energy requirements: heart, brain, and skeletal muscle.1 Publication

    Gene expression databases

    ArrayExpressiQ9NVV4.
    BgeeiQ9NVV4.
    GenevestigatoriQ9NVV4.

    Organism-specific databases

    HPAiHPA038620.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself3EBI-2556166,EBI-2556166
    Azi2Q9QYP62EBI-2556166,EBI-6115874From a different organism.
    CALCOCO2Q131372EBI-2556166,EBI-739580
    TBK1Q9UHD22EBI-2556166,EBI-356402

    Protein-protein interaction databases

    BioGridi120452. 6 interactions.
    IntActiQ9NVV4. 5 interactions.
    MINTiMINT-4831364.
    STRINGi9606.ENSP00000263063.

    Structurei

    Secondary structure

    1
    582
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi64 – 7512
    Beta strandi77 – 826
    Helixi90 – 956
    Helixi96 – 983
    Beta strandi104 – 1074
    Beta strandi109 – 1179
    Helixi125 – 1284
    Helixi174 – 1807
    Beta strandi183 – 1853
    Helixi186 – 19712
    Helixi201 – 21818
    Turni219 – 2213
    Beta strandi226 – 2305
    Helixi231 – 2333
    Beta strandi244 – 2496
    Helixi277 – 29418
    Beta strandi299 – 3057
    Beta strandi307 – 3104
    Beta strandi312 – 3176
    Turni318 – 3203
    Beta strandi323 – 3275
    Helixi333 – 34412
    Helixi348 – 36316
    Helixi377 – 38913
    Helixi403 – 4064
    Helixi437 – 44711
    Helixi448 – 4503
    Helixi492 – 51019
    Helixi528 – 5303

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3PQ1X-ray3.10A/B44-538[»]
    ProteinModelPortaliQ9NVV4.
    SMRiQ9NVV4. Positions 62-532.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9NVV4.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini437 – 48347PAP-associatedAdd
    BLAST

    Sequence similaritiesi

    Belongs to the DNA polymerase type-B-like family.Curated
    Contains 1 PAP-associated domain.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG5260.
    HOGENOMiHOG000115438.
    HOVERGENiHBG082104.
    KOiK18060.
    OMAiDAEDKCI.
    OrthoDBiEOG7353WD.
    PhylomeDBiQ9NVV4.
    TreeFamiTF354308.

    Family and domain databases

    InterProiIPR002058. PAP_assoc.
    [Graphical view]
    PfamiPF03828. PAP_assoc. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9NVV4-1) [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

    MAVPGVGLLT RLNLCARRRT RVQRPIVRLL SCPGTVAKDL RRDEQPSGSV    50
    ETGFEDKIPK RRFSEMQNER REQAQRTVLI HCPEKISENK FLKYLSQFGP 100
    INNHFFYESF GLYAVVEFCQ KESIGSLQNG THTPSTAMET AIPFRSRFFN 150
    LKLKNQTSER SRVRSSNQLP RSNKQLFELL CYAESIDDQL NTLLKEFQLT 200
    EENTKLRYLT CSLIEDMAAA YFPDCIVRPF GSSVNTFGKL GCDLDMFLDL 250
    DETRNLSAHK ISGNFLMEFQ VKNVPSERIA TQKILSVLGE CLDHFGPGCV 300
    GVQKILNARC PLVRFSHQAS GFQCDLTTNN RIALTSSELL YIYGALDSRV 350
    RALVFSVRCW ARAHSLTSSI PGAWITNFSL TMMVIFFLQR RSPPILPTLD 400
    SLKTLADAED KCVIEGNNCT FVRDLSRIKP SQNTETLELL LKEFFEYFGN 450
    FAFDKNSINI RQGREQNKPD SSPLYIQNPF ETSLNISKNV SQSQLQKFVD 500
    LARESAWILQ QEDTDRPSIS SNRPWGLVSL LLPSAPNRKS FTKKKSNKFA 550
    IETVKNLLES LKGNRTENFT KTSGKRTIST QT 582
    Length:582
    Mass (Da):66,172
    Last modified:October 1, 2000 - v1
    Checksum:iEBA5BECEA39A5090
    GO
    Isoform 2 (identifier: Q9NVV4-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-52: MAVPGVGLLT...DEQPSGSVET → MAWAKKVGGR...QELGAADKQG

    Note: No experimental confirmation available.

    Show »
    Length:712
    Mass (Da):78,833
    Checksum:i90B570568F0B7A26
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti507 – 5071W → L in BAB13981. (PubMed:14702039)Curated
    Sequence conflicti554 – 5541V → A in BAB13981. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti162 – 1621R → C.
    Corresponds to variant rs1047991 [ dbSNP | Ensembl ].
    VAR_027601
    Natural varianti221 – 2211Y → H.1 Publication
    Corresponds to variant rs17855118 [ dbSNP | Ensembl ].
    VAR_027602
    Natural varianti419 – 4191C → R.1 Publication
    Corresponds to variant rs17857517 [ dbSNP | Ensembl ].
    VAR_027603
    Natural varianti478 – 4781N → D in SPAX4. 1 Publication
    VAR_064907
    Natural varianti546 – 5461S → N.1 Publication
    Corresponds to variant rs17855116 [ dbSNP | Ensembl ].
    VAR_027604

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 5252MAVPG…GSVET → MAWAKKVGGRAGQGRSLSRC DPIILDPEWLYGPPEGEGGP EGVGGETRASIHPPLRTGRH HQKVNHNIRGPEGSAKDAAP GGGGHHQAGPGQRGDEDGAL QHLCGGGGGVGVSVGRGTGT SVAAEHPSLQVKLLELQELV LRLAGDHNEGHGKFLAAAQN PADDPAPGAPAPQELGAADK QG in isoform 2. 1 PublicationVSP_020724Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB194709 mRNA. Translation: BAD98252.1.
    AY364242 mRNA. Translation: AAQ76801.1.
    AK001348 mRNA. Translation: BAA91641.1.
    AK022188 mRNA. Translation: BAB13981.1.
    AL122121 mRNA. Translation: CAH56395.1.
    AL353796, AL161651 Genomic DNA. Translation: CAH72262.1.
    AL161651, AL353796 Genomic DNA. Translation: CAI14218.1.
    CH471072 Genomic DNA. Translation: EAW86014.1.
    CH471072 Genomic DNA. Translation: EAW86015.1.
    BC061703 mRNA. Translation: AAH61703.1.
    CCDSiCCDS7165.1. [Q9NVV4-1]
    RefSeqiNP_060579.3. NM_018109.3. [Q9NVV4-1]
    UniGeneiHs.173946.

    Genome annotation databases

    EnsembliENST00000263063; ENSP00000263063; ENSG00000107951. [Q9NVV4-1]
    GeneIDi55149.
    KEGGihsa:55149.
    UCSCiuc001iva.4. human. [Q9NVV4-1]
    uc001ivb.4. human. [Q9NVV4-2]

    Polymorphism databases

    DMDMi74753002.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB194709 mRNA. Translation: BAD98252.1 .
    AY364242 mRNA. Translation: AAQ76801.1 .
    AK001348 mRNA. Translation: BAA91641.1 .
    AK022188 mRNA. Translation: BAB13981.1 .
    AL122121 mRNA. Translation: CAH56395.1 .
    AL353796 , AL161651 Genomic DNA. Translation: CAH72262.1 .
    AL161651 , AL353796 Genomic DNA. Translation: CAI14218.1 .
    CH471072 Genomic DNA. Translation: EAW86014.1 .
    CH471072 Genomic DNA. Translation: EAW86015.1 .
    BC061703 mRNA. Translation: AAH61703.1 .
    CCDSi CCDS7165.1. [Q9NVV4-1 ]
    RefSeqi NP_060579.3. NM_018109.3. [Q9NVV4-1 ]
    UniGenei Hs.173946.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3PQ1 X-ray 3.10 A/B 44-538 [» ]
    ProteinModelPortali Q9NVV4.
    SMRi Q9NVV4. Positions 62-532.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 120452. 6 interactions.
    IntActi Q9NVV4. 5 interactions.
    MINTi MINT-4831364.
    STRINGi 9606.ENSP00000263063.

    PTM databases

    PhosphoSitei Q9NVV4.

    Polymorphism databases

    DMDMi 74753002.

    Proteomic databases

    MaxQBi Q9NVV4.
    PaxDbi Q9NVV4.
    PRIDEi Q9NVV4.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000263063 ; ENSP00000263063 ; ENSG00000107951 . [Q9NVV4-1 ]
    GeneIDi 55149.
    KEGGi hsa:55149.
    UCSCi uc001iva.4. human. [Q9NVV4-1 ]
    uc001ivb.4. human. [Q9NVV4-2 ]

    Organism-specific databases

    CTDi 55149.
    GeneCardsi GC10M030598.
    HGNCi HGNC:25532. MTPAP.
    HPAi HPA038620.
    MIMi 613669. gene.
    613672. phenotype.
    neXtProti NX_Q9NVV4.
    Orphaneti 254343. Autosomal recessive spastic ataxia - optic atrophy - dysarthria.
    PharmGKBi PA164723192.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5260.
    HOGENOMi HOG000115438.
    HOVERGENi HBG082104.
    KOi K18060.
    OMAi DAEDKCI.
    OrthoDBi EOG7353WD.
    PhylomeDBi Q9NVV4.
    TreeFami TF354308.

    Miscellaneous databases

    EvolutionaryTracei Q9NVV4.
    GenomeRNAii 55149.
    NextBioi 58876.
    PROi Q9NVV4.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9NVV4.
    Bgeei Q9NVV4.
    Genevestigatori Q9NVV4.

    Family and domain databases

    InterProi IPR002058. PAP_assoc.
    [Graphical view ]
    Pfami PF03828. PAP_assoc. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification of a novel human nuclear-encoded mitochondrial poly(A) polymerase."
      Tomecki R., Dmochowska A., Gewartowski K., Dziembowski A., Stepien P.P.
      Nucleic Acids Res. 32:6001-6014(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      Tissue: Cervix carcinoma.
    2. "Human mitochondrial mRNAs are stabilized with polyadenylation regulated by mitochondria-specific poly(A) polymerase and polynucleotide phosphorylase."
      Nagaike T., Suzuki T., Katoh T., Ueda T.
      J. Biol. Chem. 280:19721-19727(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION.
    3. "NovelFam3000 -- uncharacterized human protein domains conserved across model organisms."
      Kemmer D., Podowski R.M., Arenillas D., Lim J., Hodges E., Roth P., Sonnhammer E.L.L., Hoeoeg C., Wasserman W.W.
      BMC Genomics 7:48-48(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    4. "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 1).
      Tissue: Brain and Mammary gland.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Testis.
    6. "The DNA sequence and comparative analysis of human chromosome 10."
      Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
      , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
      Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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] (ISOFORM 1), VARIANTS HIS-221; ARG-419 AND ASN-546.
    9. "Degradation of histone mRNA requires oligouridylation followed by decapping and simultaneous degradation of the mRNA both 5' to 3' and 3' to 5'."
      Mullen T.E., Marzluff W.F.
      Genes Dev. 22:50-65(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN HISTONE MRNA DEGRADATION ACTIVITY, SUBCELLULAR LOCATION.
    10. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-90, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Structural basis for dimerization and activity of human PAPD1, a noncanonical poly(A) polymerase."
      Bai Y., Srivastava S.K., Chang J.H., Manley J.L., Tong L.
      Mol. Cell 41:311-320(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 44-538, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF 221-TYR-PHE-222; PHE-230; 259-HIS--ILE-261; 294-HIS--PRO-297; LEU-312; ASP-325 AND PHE-378.
    13. Cited for: VARIANT SPAX4 ASP-478, CATALYTIC ACTIVITY, FUNCTION.

    Entry informationi

    Entry nameiPAPD1_HUMAN
    AccessioniPrimary (citable) accession number: Q9NVV4
    Secondary accession number(s): D3DRX0
    , Q659E3, Q6P7E5, Q9HA74
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 3, 2006
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 109 of the entry and version 1 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 10
      Human chromosome 10: 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. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3