Q9NVV4 (PAPD1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	582 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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	Defects in MTPAP are the cause of spastic ataxia autosomal recessive type 4 (SPAX4) [MIM:613672]. A slowly progressive neurodegenerative disease characterized by cerebellar ataxia, spastic paraparesis, dysarthria, and optic atrophy. Note=Affected individuals exhibit a drastic decrease in poly(A) tail length of representative 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 process	Transcription mRNA processing
Cellular component	Cytoplasm Mitochondrion
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation Neurodegeneration
Domain	Transit peptide
Ligand	ATP-binding Magnesium Manganese Metal-binding Nucleotide-binding RNA-binding
Molecular function	Nucleotidyltransferase Transferase
PTM	Acetylation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cell 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-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	Golgi apparatus 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 function	ATP binding Inferred from direct assay Ref.12. Source: UniProtKB RNA binding Inferred from electronic annotation. Source: UniProtKB-KW UTP binding Inferred from direct assay Ref.12. Source: UniProtKB magnesium ion binding Inferred from direct assay Ref.12. Source: UniProtKB manganese ion binding Inferred from direct assay Ref.12. Source: UniProtKB polynucleotide adenylyltransferase activity Inferred from direct assay Ref.12. Source: UniProtKB protein homodimerization activity Inferred from physical interaction Ref.12. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		3	EBI-2556166,EBI-2556166

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 37

37

Mitochondrion Potential

Chain

38 – 582

545

Poly(A) RNA polymerase, mitochondrial

PRO_0000250689

Regions

Domain

437 – 483

47

PAP-associated

Nucleotide binding

107 – 109

3

ATP Potential

Nucleotide binding

241 – 242

2

ATP Potential

Sites

Metal binding

243

1

Magnesium or manganese; catalytic By similarity

Metal binding

245

1

Magnesium or manganese; catalytic By similarity

Amino acid modifications

Modified residue

90

1

N6-acetyllysine Ref.10

Natural variations

Alternative sequence

1 – 52

52

MAVPG…GSVET → MAWAKKVGGRAGQGRSLSRC DPIILDPEWLYGPPEGEGGP EGVGGETRASIHPPLRTGRH HQKVNHNIRGPEGSAKDAAP GGGGHHQAGPGQRGDEDGAL QHLCGGGGGVGVSVGRGTGT SVAAEHPSLQVKLLELQELV LRLAGDHNEGHGKFLAAAQN PADDPAPGAPAPQELGAADK QG in isoform 2.

VSP_020724

Natural variant

162

1

R → C.
Corresponds to variant rs1047991 [ dbSNP | Ensembl ].

VAR_027601

Natural variant

221

1

Y → H. Ref.8
Corresponds to variant rs17855118 [ dbSNP | Ensembl ].

VAR_027602

Natural variant

419

1

C → R. Ref.8
Corresponds to variant rs17857517 [ dbSNP | Ensembl ].

VAR_027603

Natural variant

478

1

N → D in SPAX4. Ref.13

VAR_064907

Natural variant

546

1

S → N. Ref.8
Corresponds to variant rs17855116 [ dbSNP | Ensembl ].

VAR_027604

Experimental info

Mutagenesis

221 – 222

2

YF → AA: Reduces dimerization.

Mutagenesis

230

1

F → A: Reduced enzyme activity. Ref.12

Mutagenesis

259 – 261

3

HKI → AAA: No effect on dimerization. Loss of dimerization and of enzyme activity; when associated with 294-AAAA-297. Ref.12

Mutagenesis

294 – 297

4

HFGP → AAGA: Reduced dimerization. Loss of dimerization and of enzyme activity; when associated with 259-AAA-261. Ref.12

Mutagenesis

312

1

L → A: Reduced enzyme activity. Ref.12

Mutagenesis

325

1

D → A: Loss of enzyme activity. Ref.12

Mutagenesis

378

1

F → A: Reduced enzyme activity. Ref.12

Sequence conflict

507

1

W → L in BAB13981. Ref.4

Sequence conflict

554

1

V → A in BAB13981. Ref.4

Secondary structure

1

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582

Helix Strand Turn

Details...

Helix

64 – 75

12

Beta strand

77 – 81

5

Helix

90 – 95

6

Beta strand

104 – 107

4

Beta strand

113 – 117

5

Helix

174 – 180

7

Beta strand

183 – 185

3

Helix

186 – 197

12

Helix

201 – 218

18

Turn

219 – 221

3

Beta strand

226 – 230

5

Beta strand

244 – 249

6

Helix

277 – 287

11

Helix

291 – 294

4

Beta strand

302 – 305

4

Beta strand

307 – 310

4

Beta strand

312 – 316

5

Beta strand

323 – 327

5

Helix

333 – 342

10

Helix

348 – 363

16

Helix

377 – 389

13

Helix

403 – 406

4

Helix

437 – 447

11

Helix

492 – 510

19

Helix

528 – 530

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: EBA5BECEA39A5090	FASTA	582	66,172
	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
	Isoform 2 [UniParc]. Checksum: 90B570568F0B7A26	FASTA	712	78,833
	10 20 30 40 50 60 MAWAKKVGGR AGQGRSLSRC DPIILDPEWL YGPPEGEGGP EGVGGETRAS IHPPLRTGRH 70 80 90 100 110 120 HQKVNHNIRG PEGSAKDAAP GGGGHHQAGP GQRGDEDGAL QHLCGGGGGV GVSVGRGTGT 130 140 150 160 170 180 SVAAEHPSLQ VKLLELQELV LRLAGDHNEG HGKFLAAAQN PADDPAPGAP APQELGAADK 190 200 210 220 230 240 QGGFEDKIPK RRFSEMQNER REQAQRTVLI HCPEKISENK FLKYLSQFGP INNHFFYESF 250 260 270 280 290 300 GLYAVVEFCQ KESIGSLQNG THTPSTAMET AIPFRSRFFN LKLKNQTSER SRVRSSNQLP 310 320 330 340 350 360 RSNKQLFELL CYAESIDDQL NTLLKEFQLT EENTKLRYLT CSLIEDMAAA YFPDCIVRPF 370 380 390 400 410 420 GSSVNTFGKL GCDLDMFLDL DETRNLSAHK ISGNFLMEFQ VKNVPSERIA TQKILSVLGE 430 440 450 460 470 480 CLDHFGPGCV GVQKILNARC PLVRFSHQAS GFQCDLTTNN RIALTSSELL YIYGALDSRV 490 500 510 520 530 540 RALVFSVRCW ARAHSLTSSI PGAWITNFSL TMMVIFFLQR RSPPILPTLD SLKTLADAED 550 560 570 580 590 600 KCVIEGNNCT FVRDLSRIKP SQNTETLELL LKEFFEYFGN FAFDKNSINI RQGREQNKPD 610 620 630 640 650 660 SSPLYIQNPF ETSLNISKNV SQSQLQKFVD LARESAWILQ QEDTDRPSIS SNRPWGLVSL 670 680 690 700 710 LLPSAPNRKS FTKKKSNKFA IETVKNLLES LKGNRTENFT KTSGKRTIST QT

References

	« Hide 'large scale' referencesShow '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: 15547249] [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: 15769737] [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: 16533400] [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: 14702039] [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: 17974005] [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. , 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: 15164054] [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. , 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: 15489334] [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: 18172165] [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., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-90, MASS SPECTROMETRY.
[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: 21269460] [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: 21292163] [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: 20970105] [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.

IPI

IPI00153051.
IPI00470416.

RefSeq

NP_060579.3. NM_018109.3.

UniGene

Hs.173946.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3PQ1	X-ray	3.10	A/B	44-538	[»]

ProteinModelPortal

Q9NVV4.

SMR

Q9NVV4. Positions 62-532.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9NVV4. 2 interactions.

STRING

Q9NVV4.

PTM databases

PhosphoSite

Q9NVV4.

Polymorphism databases

DMDM

74753002.

Proteomic databases

PRIDE

Q9NVV4.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000263063; ENSP00000263063; ENSG00000107951.

GeneID

55149.

KEGG

hsa:55149.

UCSC

uc001iva.2. human.
uc001ivb.2. human.

Organism-specific databases

CTD

55149.

GeneCards

GC10M030642.

H-InvDB

HIX0008743.

HGNC

HGNC:25532. MTPAP.

HPA

HPA038620.

MIM

613669. gene.
613672. phenotype.

neXtProt

NX_Q9NVV4.

PharmGKB

PA164723192.

GenAtlas

Search...

Phylogenomic databases

GeneTree

ENSGT00550000074490.

HOVERGEN

HBG082104.

OMA

PGCVGVQ.

OrthoDB

EOG45TCN5.

PhylomeDB

Q9NVV4.

Gene expression databases

ArrayExpress

Q9NVV4.

Bgee

Q9NVV4.

Genevestigator

Q9NVV4.

GermOnline

ENSG00000107951. Homo sapiens.

Family and domain databases

InterPro

IPR002058. PAP_assoc.
[Graphical view]

Pfam

PF03828. PAP_assoc. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

58876.

SOURCE

Search...

Entry information

Entry name

PAPD1_HUMAN

Accession

Primary (citable) accession number: Q9NVV4
Secondary accession number(s): D3DRX0 , Q659E3, Q6P7E5, Q9HA74

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 3, 2006
Last sequence update:	October 1, 2000
Last modified:	January 25, 2012
This is version 84 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.