Q5XG87 (PAPD7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
DNA polymerase sigma
EC=2.7.7.7

Alternative name(s):
DNA polymerase kappa
LAK-1
PAP-associated domain-containing protein 7
Terminal uridylyltransferase 5
Short name=TUTase 5
Topoisomerase-related function protein 4-1
Short name=TRF4-1

Gene names

Name:	PAPD7
Synonyms:	POLS, TRF4

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	542 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	DNA polymerase, probably involved in DNA repair. May play a role in sister chromatid cohesion. Does not play a role in replication-dependent histone mRNA degradation. Ref.7 Ref.9
Catalytic activity	Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).
Cofactor	Magnesium or manganese By similarity.
Subcellular location	Nucleus Probable.
Sequence similarities	Belongs to the DNA polymerase type-B-like family. Contains 1 PAP-associated domain.
Sequence caution	The sequence AAD45198.1 differs from that shown. Reason: Frameshift at position 474.

Ontologies

Keywords
Biological process	Cell cycle Cell division DNA synthesis Mitosis
Cellular component	Nucleus
Coding sequence diversity	Polymorphism
Ligand	DNA-binding Magnesium Manganese Metal-binding
Molecular function	DNA-directed DNA polymerase Nucleotidyltransferase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	DNA replication Inferred from electronic annotation. Source: UniProtKB-KW cell division Inferred from electronic annotation. Source: UniProtKB-KW double-strand break repair Non-traceable author statement Ref.1. Source: UniProtKB mitotic chromosome condensation Non-traceable author statement Ref.1. Source: UniProtKB response to drug Inferred from direct assay Ref.1. Source: UniProtKB sister chromatid cohesion Traceable author statement Ref.1. Source: UniProtKB
Cellular component	nucleus Inferred from direct assay Ref.1. Source: UniProtKB
Molecular function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW DNA-directed DNA polymerase activity Inferred from electronic annotation. Source: UniProtKB-KW SMC protein binding Traceable author statement Ref.1. Source: UniProtKB metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 542	542	DNA polymerase sigma		PRO_0000120308
Regions
	Domain	178 – 238	61	PAP-associated
	Compositional bias	346 – 372	27	Ser-rich
Sites
	Metal binding	47	1	Magnesium or manganese; catalytic By similarity
	Metal binding	49	1	Magnesium or manganese; catalytic By similarity
Natural variations
	Natural variant	326	1	N → S. Ref.3 Corresponds to variant rs28381415 [ dbSNP | Ensembl ].		VAR_021175
	Natural variant	396	1	G → S. Ref.3 Corresponds to variant rs28381418 [ dbSNP | Ensembl ].		VAR_021176

Sequences

	Sequence		Length	Mass (Da)
	Q5XG87 [UniParc]. Last modified February 1, 2005. Version 2. Checksum: 233DA7E2222C2FB0	FASTA	542	59,874
	10 20 30 40 50 60 MSPCPEEAAM RREVVKRIET VVKDLWPTAD VQIFGSFSTG LYLPTSDIDL VVFGKWERPP 70 80 90 100 110 120 LQLLEQALRK HNVAEPCSIK VLDKATVPII KLTDQETEVK VDISFNMETG VRAAEFIKNY 130 140 150 160 170 180 MKKYSLLPYL ILVLKQFLLQ RDLNEVFTGG ISSYSLILMA ISFLQLHPRI DARRADENLG 190 200 210 220 230 240 MLLVEFFELY GRNFNYLKTG IRIKEGGAYI AKEEIMKAMT SGYRPSMLCI EDPLLPGNDV 250 260 270 280 290 300 GRSSYGAMQV KQVFDYAYIV LSHAVSPLAR SYPNRDAEST LGRIIKVTQE VIDYRRWIKE 310 320 330 340 350 360 KWGSKAHPSP GMDSRIKIKE RIATCNGEQT QNREPESPYG QRLTLSLSSP QLLSSGSSAS 370 380 390 400 410 420 SVSSLSGSDV DSDTPPCTTP SVYQFSLQAP APLMAGLPTA LPMPSGKPQP TTSRTLIMTT 430 440 450 460 470 480 NNQTRFTIPP PTLGVAPVPC RQAGVEGTAS LKAVHHMSSP AIPSASPNPL SSPHLYHKQH 490 500 510 520 530 540 NGMKLSMKGS HGHTQGGGYS SVGSGGVRPP VGNRGHHQYN RTGWRRKKHT HTRDSLPVSL SR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The topoisomerase-related function gene TRF4 affects cellular sensitivity to the antitumor agent camptothecin." Walowsky C., Fitzhugh D.J., Castano I.B., Ju J.Y., Levin N.A., Christman M.F. J. Biol. Chem. 274:7302-7308(1999) [PubMed: 10066793] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"mLT positive LAK-cell clone No. 1." Abe Y., Takaoka Y. Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	NIEHS SNPs program Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS SER-326 AND SER-396.
[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]. Tissue: Brain.
[5]	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].
[6]	"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]. Tissue: Cerebellum and Lung.
[7]	"Pol kappa: a DNA polymerase required for sister chromatid cohesion." Wang Z., Castano I.B., De Las Penas A., Adams C., Christman M.F. Science 289:774-779(2000) [PubMed: 10926539] [Abstract] Cited for: FUNCTION.
[8]	"Evidence that replication fork components catalyze establishment of cohesion between sister chromatids." Carson D.R., Christman M.F. Proc. Natl. Acad. Sci. U.S.A. 98:8270-8275(2001) [PubMed: 11459963] [Abstract] Cited for: REVIEW.
[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: ABSENCE OF FUNCTION IN HISTONE MRNA DEGRADATION ACTIVITY.
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF089896 mRNA. Translation: AAD45198.1. Sequence problems. AB005754 mRNA. Translation: BAA24434.2. AY623114 Genomic DNA. Translation: AAT38110.1. AK289857 mRNA. Translation: BAF82546.1. CH471102 Genomic DNA. Translation: EAX08101.1. BC084567 mRNA. Translation: AAH84567.2. BC117137 mRNA. Translation: AAI17138.1. BC126106 mRNA. Translation: AAI26107.1.
IPI	IPI00418630.
RefSeq	NP_001165276.1. NM_001171805.1. NP_001165277.1. NM_001171806.1. NP_008930.1. NM_006999.4.
UniGene	Hs.481542.
3D structure databases
ProteinModelPortal	Q5XG87.
SMR	Q5XG87. Positions 1-287.
ModBase	Search...
Protein-protein interaction databases
STRING	Q5XG87.
PTM databases
PhosphoSite	Q5XG87.
Polymorphism databases
DMDM	60392922.
Proteomic databases
PRIDE	Q5XG87.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000230859; ENSP00000230859; ENSG00000112941.
GeneID	11044.
KEGG	hsa:11044.
UCSC	uc003jdx.1. human.
Organism-specific databases
CTD	11044.
GeneCards	GC05P006714.
H-InvDB	HIX0031938.
HGNC	HGNC:16705. PAPD7.
MIM	605198. gene.
neXtProt	NX_Q5XG87.
PharmGKB	PA33523.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG08372.
GeneTree	ENSGT00400000022055.
HOGENOM	HBG714944.
HOVERGEN	HBG053636.
InParanoid	Q5XG87.
OMA	DNRIKIK.
OrthoDB	EOG4N04DQ.
PhylomeDB	Q5XG87.
Gene expression databases
ArrayExpress	Q5XG87.
Bgee	Q5XG87.
CleanEx	HS_POLS.
Genevestigator	Q5XG87.
GermOnline	ENSG00000112941. Homo sapiens.
Family and domain databases
InterPro	IPR002934. Nucleotidyltransferase. IPR002058. PAP_assoc. [Graphical view]
KO	K03514.
Pfam	PF01909. NTP_transf_2. 1 hit. PF03828. PAP_assoc. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	41972.
SOURCE	Search...

Entry information

Entry name

PAPD7_HUMAN

Accession

Primary (citable) accession number: Q5XG87
Secondary accession number(s): A8K1E2 , O43289, Q17RZ1, Q9Y6C1

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 2005
Last sequence update:	February 1, 2005
Last modified:	December 14, 2011
This is version 71 of the entry and version 2 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.