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Q9NVV4

- PAPD1_HUMAN

UniProt

Q9NVV4 - PAPD1_HUMAN

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Protein
Poly(A) RNA polymerase, mitochondrial
Gene
MTPAP, PAPD1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 UTP

Sites

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

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi107 – 1093ATP Reviewed prediction
Nucleotide bindingi241 – 2422ATP Reviewed prediction

GO - Molecular functioni

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

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

Cytoplasm. Mitochondrion 3 Publications

GO - Cellular componenti

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

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.
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 (1 Publication).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. 1 Publication
Mutagenesisi294 – 2974HFGP → AAGA: Reduced dimerization. Loss of dimerization and of enzyme activity; when associated with 259-AAA-261. 1 Publication
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 – 3737Mitochondrion Reviewed prediction
Add
BLAST
Chaini38 – 582545Poly(A) RNA polymerase, mitochondrial
PRO_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

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.

Miscellaneous databases

EvolutionaryTraceiQ9NVV4.

Family & Domainsi

Domains and Repeats

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

Sequence similaritiesi

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

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.
VSP_020724Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti507 – 5071W → L in BAB13981. 1 Publication
Sequence conflicti554 – 5541V → A in BAB13981. 1 Publication

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]
ENST00000358107; ENSP00000350820; ENSG00000107951. [Q9NVV4-2]
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 ]
ENST00000358107 ; ENSP00000350820 ; ENSG00000107951 . [Q9NVV4-2 ]
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

« Hide 'large scale' publications
  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: July 9, 2014
This is version 108 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

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