Q6PIY7 (GLD2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	484 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	mRNA processing
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing
Ligand	ATP-binding Magnesium Manganese Metal-binding Nucleotide-binding
Molecular function	Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	RNA polyadenylation Inferred from direct assay Ref.4. Source: UniProtKB histone mRNA catabolic process Inferred from mutant phenotype Ref.6. Source: UniProtKB mRNA processing Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nuclear RNA-directed RNA polymerase complex Inferred by curator Ref.4. Source: UniProtKB
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW polynucleotide adenylyltransferase activity Inferred from direct assay Ref.4. Source: UniProtKB
Complete GO annotation...

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 484	484	Poly(A) RNA polymerase GLD2		PRO_0000341549
Regions
	Domain	386 – 440	55	PAP-associated
	Motif	76 – 92	17	Nuclear localization signal Potential
Sites
	Metal binding	213	1	Magnesium or manganese; catalytic By similarity
	Metal binding	215	1	Magnesium or manganese; catalytic By similarity
Amino acid modifications
	Modified residue	62	1	Phosphoserine Ref.8
	Modified residue	69	1	Phosphoserine Ref.7
Natural variations
	Alternative sequence	225 – 228	4	Missing in isoform 2.		VSP_034324
Experimental info
	Sequence conflict	9	1	R → H in BAC04629. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: 26167D53ABDA979D	FASTA	484	56,028
	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
	Isoform 2 [UniParc]. Checksum: 5E765A67D255F232	FASTA	480	55,502
	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 KEEPVNQKTE ARHILTLVHK 250 260 270 280 290 300 HFCTRLSGYI ERPQLIRAKV PIVKFRDKVS CVEFDLNVNN IVGIRNTFLL RTYAYLENRV 310 320 330 340 350 360 RPLVLVIKKW ASHHQINDAS RGTLSSYSLV LMVLHYLQTL PEPILPSLQK IYPESFSPAI 370 380 390 400 410 420 QLHLVHQAPC NVPPYLSKNE SNLGDLLLGF LKYYATEFDW NSQMISVREA KAIPRPDGIE 430 440 450 460 470 480 WRNKYICVEE PFDGTNTARA VHEKQKFDMI KDQFLKSWHR LKNKRDLNSI LPVRAAVLKR

References

	« Hide 'large scale' referencesShow '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. , 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. , 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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.
IPI	IPI00167560. IPI00895778.
RefSeq	NP_001107865.1. NM_001114393.1. NP_001107866.1. NM_001114394.1. NP_776158.2. NM_173797.3.
UniGene	Hs.418198.
3D structure databases
HSSP	HSSP built from PDB template 2B4V based on UniProtKB Q86MV5.
ProteinModelPortal	Q6PIY7.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q6PIY7. 3 interactions.
STRING	9606.ENSP00000296783.
PTM databases
PhosphoSite	Q6PIY7.
Polymorphism databases
DMDM	74737798.
Proteomic databases
PaxDb	Q6PIY7.
PRIDE	Q6PIY7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000296783; ENSP00000296783; ENSG00000164329. ENST00000423041; ENSP00000393412; ENSG00000164329. ENST00000428308; ENSP00000396861; ENSG00000164329. ENST00000453514; ENSP00000397563; ENSG00000164329.
GeneID	167153.
KEGG	hsa:167153.
UCSC	uc003kga.2. human. uc003kgb.2. human.
Organism-specific databases
CTD	167153.
GeneCards	GC05P078944.
HGNC	HGNC:26776. PAPD4.
MIM	614121. gene.
neXtProt	NX_Q6PIY7.
PharmGKB	PA134918975.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG5260.
HOGENOM	HOG000088606.
HOVERGEN	HBG097533.
InParanoid	Q6PIY7.
KO	K14079.
OMA	NQKTEAR.
PhylomeDB	Q6PIY7.
Gene expression databases
ArrayExpress	Q6PIY7.
Bgee	Q6PIY7.
CleanEx	HS_PAPD4.
Genevestigator	Q6PIY7.
Family and domain databases
InterPro	IPR002058. PAP_assoc. [Graphical view]
Pfam	PF03828. PAP_assoc. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	PAPD4. human.
GenomeRNAi	167153.
NextBio	88659.
SOURCE	Search...

Entry information

Entry name

GLD2_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 68 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.