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Q9NVV4 (PAPD1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Poly(A) RNA polymerase, mitochondrial

Short name=PAP
EC=2.7.7.19
Alternative name(s):
PAP-associated domain-containing protein 1
Polynucleotide adenylyltransferase
Terminal uridylyltransferase 1
Short name=TUTase 1
mtPAP
Gene names
Name:MTPAP
Synonyms:PAPD1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length582 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.2 Ref.9 Ref.12 Ref.13

Catalytic activity

ATP + RNA(n) = diphosphate + RNA(n+1). Ref.12 Ref.13

Cofactor

Magnesium or manganese. Ref.12

Subunit structure

Homodimer. Ref.12

Subcellular location

Cytoplasm. Mitochondrion Ref.1 Ref.2 Ref.9.

Tissue specificity

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

Involvement in disease

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 (Ref.13). Ref.13

Sequence similarities

Belongs to the DNA polymerase type-B-like family.

Contains 1 PAP-associated domain.

Biophysicochemical properties

Kinetic parameters:

KM=0.1 mM for ATP Ref.12

KM=0.7 mM for UTP

Ontologies

Keywords
   Biological processmRNA processing
Transcription
   Cellular componentCytoplasm
Mitochondrion
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
Neurodegeneration
   DomainTransit peptide
   LigandATP-binding
Magnesium
Manganese
Metal-binding
Nucleotide-binding
RNA-binding
   Molecular functionNucleotidyltransferase
Transferase
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell death

Inferred from electronic annotation. Source: UniProtKB-KW

histone mRNA catabolic process

Inferred from mutant phenotype Ref.9. Source: UniProtKB

mRNA polyadenylation

Inferred from direct assay Ref.12. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentGolgi apparatus

Inferred from direct assay. Source: HPA

cytoplasm

Inferred from direct assay. Source: HPA

mitochondrion

Inferred from direct assay. Source: HPA

nucleus

Inferred from direct assay. Source: HPA

plasma membrane

Inferred from direct assay. Source: HPA

   Molecular_functionATP binding

Inferred from direct assay Ref.12. Source: UniProtKB

UTP binding

Inferred from direct assay Ref.12. Source: UniProtKB

identical protein binding

Inferred from physical interaction Ref.12. Source: IntAct

magnesium ion binding

Inferred from direct assay Ref.12. Source: UniProtKB

manganese ion binding

Inferred from direct assay Ref.12. Source: UniProtKB

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

polynucleotide adenylyltransferase activity

Inferred from direct assay Ref.12. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 21903422. Source: IntAct

protein homodimerization activity

Inferred from physical interaction Ref.12. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

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

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9NVV4-1)

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.
Isoform 2 (identifier: Q9NVV4-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-52: MAVPGVGLLT...DEQPSGSVET → MAWAKKVGGR...QELGAADKQG
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3737Mitochondrion Potential
Chain38 – 582545Poly(A) RNA polymerase, mitochondrial
PRO_0000250689

Regions

Domain437 – 48347PAP-associated
Nucleotide binding107 – 1093ATP Potential
Nucleotide binding241 – 2422ATP Potential

Sites

Metal binding2431Magnesium or manganese; catalytic By similarity
Metal binding2451Magnesium or manganese; catalytic By similarity

Amino acid modifications

Modified residue901N6-acetyllysine Ref.10

Natural variations

Alternative sequence1 – 5252MAVPG…GSVET → MAWAKKVGGRAGQGRSLSRC DPIILDPEWLYGPPEGEGGP EGVGGETRASIHPPLRTGRH HQKVNHNIRGPEGSAKDAAP GGGGHHQAGPGQRGDEDGAL QHLCGGGGGVGVSVGRGTGT SVAAEHPSLQVKLLELQELV LRLAGDHNEGHGKFLAAAQN PADDPAPGAPAPQELGAADK QG in isoform 2.
VSP_020724
Natural variant1621R → C.
Corresponds to variant rs1047991 [ dbSNP | Ensembl ].
VAR_027601
Natural variant2211Y → H. Ref.8
Corresponds to variant rs17855118 [ dbSNP | Ensembl ].
VAR_027602
Natural variant4191C → R. Ref.8
Corresponds to variant rs17857517 [ dbSNP | Ensembl ].
VAR_027603
Natural variant4781N → D in SPAX4. Ref.13
VAR_064907
Natural variant5461S → N. Ref.8
Corresponds to variant rs17855116 [ dbSNP | Ensembl ].
VAR_027604

Experimental info

Mutagenesis221 – 2222YF → AA: Reduces dimerization.
Mutagenesis2301F → A: Reduced enzyme activity. Ref.12
Mutagenesis259 – 2613HKI → AAA: No effect on dimerization. Loss of dimerization and of enzyme activity; when associated with 294-AAAA-297. Ref.12
Mutagenesis294 – 2974HFGP → AAGA: Reduced dimerization. Loss of dimerization and of enzyme activity; when associated with 259-AAA-261. Ref.12
Mutagenesis3121L → A: Reduced enzyme activity. Ref.12
Mutagenesis3251D → A: Loss of enzyme activity. Ref.12
Mutagenesis3781F → A: Reduced enzyme activity. Ref.12
Sequence conflict5071W → L in BAB13981. Ref.4
Sequence conflict5541V → A in BAB13981. Ref.4

Secondary structure

..................................................... 582
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: EBA5BECEA39A5090

FASTA58266,172
        10         20         30         40         50         60 
MAVPGVGLLT RLNLCARRRT RVQRPIVRLL SCPGTVAKDL RRDEQPSGSV ETGFEDKIPK 

        70         80         90        100        110        120 
RRFSEMQNER REQAQRTVLI HCPEKISENK FLKYLSQFGP INNHFFYESF GLYAVVEFCQ 

       130        140        150        160        170        180 
KESIGSLQNG THTPSTAMET AIPFRSRFFN LKLKNQTSER SRVRSSNQLP RSNKQLFELL 

       190        200        210        220        230        240 
CYAESIDDQL NTLLKEFQLT EENTKLRYLT CSLIEDMAAA YFPDCIVRPF GSSVNTFGKL 

       250        260        270        280        290        300 
GCDLDMFLDL DETRNLSAHK ISGNFLMEFQ VKNVPSERIA TQKILSVLGE CLDHFGPGCV 

       310        320        330        340        350        360 
GVQKILNARC PLVRFSHQAS GFQCDLTTNN RIALTSSELL YIYGALDSRV RALVFSVRCW 

       370        380        390        400        410        420 
ARAHSLTSSI PGAWITNFSL TMMVIFFLQR RSPPILPTLD SLKTLADAED KCVIEGNNCT 

       430        440        450        460        470        480 
FVRDLSRIKP SQNTETLELL LKEFFEYFGN FAFDKNSINI RQGREQNKPD SSPLYIQNPF 

       490        500        510        520        530        540 
ETSLNISKNV SQSQLQKFVD LARESAWILQ QEDTDRPSIS SNRPWGLVSL LLPSAPNRKS 

       550        560        570        580 
FTKKKSNKFA IETVKNLLES LKGNRTENFT KTSGKRTIST QT 

« Hide

Isoform 2 [UniParc].

Checksum: 90B570568F0B7A26
Show »

FASTA71278,833

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"Defective mitochondrial mRNA maturation is associated with spastic ataxia."
Crosby A.H., Patel H., Chioza B.A., Proukakis C., Gurtz K., Patton M.A., Sharifi R., Harlalka G., Simpson M.A., Dick K., Reed J.A., Al-Memar A., Chrzanowska-Lightowlers Z.M., Cross H.E., Lightowlers R.N.
Am. J. Hum. Genet. 87:655-660(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SPAX4 ASP-478, CATALYTIC ACTIVITY, FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS7165.1. [Q9NVV4-1]
RefSeqNP_060579.3. NM_018109.3. [Q9NVV4-1]
UniGeneHs.173946.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3PQ1X-ray3.10A/B44-538[»]
ProteinModelPortalQ9NVV4.
SMRQ9NVV4. Positions 62-532.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid120452. 6 interactions.
IntActQ9NVV4. 5 interactions.
MINTMINT-4831364.
STRING9606.ENSP00000263063.

PTM databases

PhosphoSiteQ9NVV4.

Polymorphism databases

DMDM74753002.

Proteomic databases

MaxQBQ9NVV4.
PaxDbQ9NVV4.
PRIDEQ9NVV4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000263063; ENSP00000263063; ENSG00000107951. [Q9NVV4-1]
ENST00000358107; ENSP00000350820; ENSG00000107951. [Q9NVV4-2]
GeneID55149.
KEGGhsa:55149.
UCSCuc001iva.4. human. [Q9NVV4-1]
uc001ivb.4. human. [Q9NVV4-2]

Organism-specific databases

CTD55149.
GeneCardsGC10M030598.
HGNCHGNC:25532. MTPAP.
HPAHPA038620.
MIM613669. gene.
613672. phenotype.
neXtProtNX_Q9NVV4.
Orphanet254343. Autosomal recessive spastic ataxia - optic atrophy - dysarthria.
PharmGKBPA164723192.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5260.
HOGENOMHOG000115438.
HOVERGENHBG082104.
KOK18060.
OMADAEDKCI.
OrthoDBEOG7353WD.
PhylomeDBQ9NVV4.
TreeFamTF354308.

Gene expression databases

ArrayExpressQ9NVV4.
BgeeQ9NVV4.
GenevestigatorQ9NVV4.

Family and domain databases

InterProIPR002058. PAP_assoc.
[Graphical view]
PfamPF03828. PAP_assoc. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9NVV4.
GenomeRNAi55149.
NextBio58876.
PROQ9NVV4.
SOURCESearch...

Entry information

Entry namePAPD1_HUMAN
AccessionPrimary (citable) accession number: Q9NVV4
Secondary accession number(s): D3DRX0 expand/collapse secondary AC list , Q659E3, Q6P7E5, Q9HA74
Entry history
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 statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM