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Q6PIY7 (GLD2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Poly(A) RNA polymerase GLD2

Short name=hGLD-2
EC=2.7.7.19
Alternative name(s):
PAP-associated domain-containing protein 4
Terminal uridylyltransferase 2
Short name=TUTase 2
Gene names
Name:PAPD4
Synonyms:GLD2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length484 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Cytoplasmic poly(A) RNA polymerase that adds successive AMP monomers to the 3'-end of specific RNAs, forming a poly(A) tail. In contrast to the canonical nuclear poly(A) RNA polymerase, it only adds poly(A) to selected cytoplasmic mRNAs. Does not play a role in replication-dependent histone mRNA degradation. Ref.6

Catalytic activity

ATP + RNA(n) = diphosphate + RNA(n+1). Ref.4

Cofactor

Magnesium or manganese By similarity.

Subunit structure

Interacts with CPEB1, CPEB2, CPSF1 and PABPC1 By similarity.

Subcellular location

Cytoplasm By similarity. Nucleus By similarity.

Tissue specificity

Expressed in brain. Within brain, it is expressed in cerebellum, hippocampus and medulla. Ref.5

Sequence similarities

Belongs to the DNA polymerase type-B-like family. GLD2 subfamily.

Contains 1 PAP-associated domain.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q6PIY7-1)

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: Q6PIY7-2)

The sequence of this isoform differs from the canonical sequence as follows:
     225-228: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 484484Poly(A) RNA polymerase GLD2
PRO_0000341549

Regions

Domain386 – 44055PAP-associated
Motif76 – 9217Nuclear localization signal Potential

Sites

Metal binding2131Magnesium or manganese; catalytic By similarity
Metal binding2151Magnesium or manganese; catalytic By similarity

Amino acid modifications

Modified residue621Phosphoserine Ref.8
Modified residue691Phosphoserine Ref.7

Natural variations

Alternative sequence225 – 2284Missing in isoform 2.
VSP_034324

Experimental info

Sequence conflict91R → H in BAC04629. Ref.1

Sequences

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

Last modified July 5, 2004. Version 1.
Checksum: 26167D53ABDA979D

FASTA48456,028
        10         20         30         40         50         60 
MFPNSILGRP PFTPNHQQHN NFFTLSPTVY SHQQLIDAQF NFQNADLSRA VSLQQLTYGN 

        70         80         90        100        110        120 
VSPIQTSASP LFRGRKRLSD EKNLPLDGKR QRFHSPHQEP TVVNQIVPLS GERRYSMPPL 

       130        140        150        160        170        180 
FHTHYVPDIV RCVPPFREIA FLEPREITLP EAKDKLSQQI LELFETCQQQ ISDLKKKELC 

       190        200        210        220        230        240 
RTQLQREIQL LFPQSRLFLV GSSLNGFGTR SSDGDLCLVV KEEPCFFQVN QKTEARHILT 

       250        260        270        280        290        300 
LVHKHFCTRL SGYIERPQLI RAKVPIVKFR DKVSCVEFDL NVNNIVGIRN TFLLRTYAYL 

       310        320        330        340        350        360 
ENRVRPLVLV IKKWASHHQI NDASRGTLSS YSLVLMVLHY LQTLPEPILP SLQKIYPESF 

       370        380        390        400        410        420 
SPAIQLHLVH QAPCNVPPYL SKNESNLGDL LLGFLKYYAT EFDWNSQMIS VREAKAIPRP 

       430        440        450        460        470        480 
DGIEWRNKYI CVEEPFDGTN TARAVHEKQK FDMIKDQFLK SWHRLKNKRD LNSILPVRAA 


VLKR 

« Hide

Isoform 2 [UniParc].

Checksum: 5E765A67D255F232
Show »

FASTA48055,502

References

« Hide 'large scale' references
[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. 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: Smooth muscle.
[2]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 (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"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 2).
Tissue: Pancreas.
[4]"Mammalian GLD-2 homologs are poly(A) polymerases."
Kwak J.E., Wang L., Ballantyne S., Kimble J., Wickens M.
Proc. Natl. Acad. Sci. U.S.A. 101:4407-4412(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME ACTIVITY.
[5]"Vertebrate GLD2 poly(A) polymerases in the germline and the brain."
Rouhana L., Wang L., Buter N., Kwak J.E., Schiltz C.A., Gonzalez T., Kelley A.E., Landry C.F., Wickens M.
RNA 11:1117-1130(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[6]"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: ABSENCE OF FUNCTION IN HISTONE MRNA DEGRADATION ACTIVITY.
[7]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-69, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[8]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK095818 mRNA. Translation: BAC04629.1.
CH471084 Genomic DNA. Translation: EAW95837.1.
BC026061 mRNA. Translation: AAH26061.1.
BC047581 mRNA. Translation: AAH47581.1.
RefSeqNP_001107865.1. NM_001114393.1.
NP_001107866.1. NM_001114394.1.
NP_776158.2. NM_173797.3.
XP_005248508.1. XM_005248451.1.
UniGeneHs.418198.

3D structure databases

ProteinModelPortalQ6PIY7.
SMRQ6PIY7. Positions 162-469.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid127943. 2 interactions.
IntActQ6PIY7. 3 interactions.
STRING9606.ENSP00000296783.

PTM databases

PhosphoSiteQ6PIY7.

Polymorphism databases

DMDM74737798.

Proteomic databases

PaxDbQ6PIY7.
PRIDEQ6PIY7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000296783; ENSP00000296783; ENSG00000164329. [Q6PIY7-1]
ENST00000423041; ENSP00000393412; ENSG00000164329. [Q6PIY7-2]
ENST00000428308; ENSP00000396861; ENSG00000164329. [Q6PIY7-1]
ENST00000453514; ENSP00000397563; ENSG00000164329. [Q6PIY7-1]
GeneID167153.
KEGGhsa:167153.
UCSCuc003kga.2. human. [Q6PIY7-2]
uc003kgb.2. human. [Q6PIY7-1]

Organism-specific databases

CTD167153.
GeneCardsGC05P078944.
HGNCHGNC:26776. PAPD4.
MIM614121. gene.
neXtProtNX_Q6PIY7.
PharmGKBPA134918975.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5260.
HOGENOMHOG000088606.
HOVERGENHBG097533.
InParanoidQ6PIY7.
KOK14079.
OMAYIERPQL.
OrthoDBEOG7DRJ2S.
PhylomeDBQ6PIY7.
TreeFamTF315661.

Gene expression databases

ArrayExpressQ6PIY7.
BgeeQ6PIY7.
CleanExHS_PAPD4.
GenevestigatorQ6PIY7.

Family and domain databases

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

Other

ChiTaRSPAPD4. human.
GenomeRNAi167153.
NextBio88659.
PROQ6PIY7.
SOURCESearch...

Entry information

Entry nameGLD2_HUMAN
AccessionPrimary (citable) accession number: Q6PIY7
Secondary accession number(s): Q86WZ2, Q8N927
Entry history
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: July 5, 2004
Last modified: March 19, 2014
This is version 76 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

MIM cross-references

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

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM