O15446 (RPA34_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
DNA-directed RNA polymerase I subunit RPA34

Alternative name(s):
A34.5
Antisense to ERCC-1 protein
Short name=ASE-1
CD3-epsilon-associated protein
Short name=CAST
Short name=CD3E-associated protein
RNA polymerase I-associated factor PAF49

Gene names

Name:	CD3EAP
Synonyms:	ASE1, CAST, PAF49

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

General annotation (Comments)

Function	DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase I which synthesizes ribosomal RNA precursors. Isoform 1 is involved in UBTF-activated transcription, presumably at a step following PIC formation. Ref.2 Ref.5 Isoform 2 has been described as a component of preformed T-cell receptor (TCR) complex. Ref.2 Ref.5
Subunit structure	Component of the RNA polymerase I (Pol I) complex consisting of at least 13 subunits. Interacts with TAF1A thereby associates with the SL1 complex. Interacts with UBTF. Interacts with POLR1E/PRAF1 through its N-terminal region By similarity. Isoform 2 interacts with CD3E. Ref.2 Ref.5
Subcellular location	Nucleus › nucleolus. Chromosome. Note: Found at the fibrillar centers of the nucleolus in interphase and during cell division it is localized to the nucleolus organizer regions of the chromosomes. Ref.1
Post-translational modification	Isoform 2 undergoes tyrosine phosphorylation upon T-cell receptor (TCR) stimulation. This phosphorylation has not been confirmed by other groups. Isoform 1 is phosphorylated on tyrosine residues in initiation-competent Pol I-beta complexes but not in Pol I-alpha complexes. Ref.2 Ref.5
Miscellaneous	It is in an antisense orientation to and overlaps the gene of the DNA repair enzyme ERCC1. This gene overlap is conserved in mouse, suggesting an important biological function.
Sequence similarities	Belongs to the eukaryotic RPA34 RNA polymerase subunit family.
Caution	It is not known whether the so-called human ASE1 and human CAST proteins represent two sides of a single gene product with sharply different functional characteristics. Experiments done with the mouse homolog protein are in favor of an implication of this gene in rRNA transcription instead of T-cell receptor signaling.

Ontologies

Keywords
Biological process	Transcription
Cellular component	Chromosome DNA-directed RNA polymerase Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	rRNA transcription Traceable author statement Ref.1. Source: ProtInc transmembrane receptor protein tyrosine kinase signaling pathway Traceable author statement Ref.2. Source: ProtInc
Cellular_component	DNA-directed RNA polymerase I complex Inferred from electronic annotation. Source: Compara RNA polymerase I transcription factor complex Traceable author statement Ref.1. Source: ProtInc chromosome Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrion Inferred from direct assay. Source: HPA
Molecular_function	DNA-directed RNA polymerase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: O15446-1)

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: O15446-2)

Also known as: CAST;

The sequence of this isoform differs from the canonical sequence as follows:
     7-7: G → GGE

Note: No experimental confirmation available. Has sharply different functional characteristics.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 510	510	DNA-directed RNA polymerase I subunit RPA34		PRO_0000228120
Regions
	Compositional bias	174 – 177	4	Poly-Lys
	Compositional bias	212 – 217	6	Poly-Lys
	Compositional bias	422 – 428	7	Poly-Lys
	Compositional bias	504 – 508	5	Poly-Gln
Amino acid modifications
	Modified residue	27	1	Phosphoserine Ref.7
	Modified residue	80	1	Phosphotyrosine Ref.5
	Modified residue	128	1	Phosphoserine Ref.7
	Modified residue	136	1	Phosphoserine Ref.7 Ref.8 Ref.10
	Modified residue	172	1	Phosphoserine Ref.7 Ref.9
	Modified residue	205	1	Phosphoserine Ref.7
	Modified residue	285	1	Phosphoserine Ref.7 Ref.9 Ref.10
	Modified residue	287	1	Phosphothreonine Ref.7
	Modified residue	309	1	Phosphoserine Ref.6
	Modified residue	490	1	Phosphoserine Ref.8
Natural variations
	Alternative sequence	7	1	G → GGE in isoform 2.		VSP_017673
	Natural variant	259	1	K → T. Corresponds to variant rs735482 [ dbSNP | Ensembl ].		VAR_051875
	Natural variant	282	1	T → A. Corresponds to variant rs3212989 [ dbSNP | Ensembl ].		VAR_051876
	Natural variant	373	1	K → E. Corresponds to variant rs762562 [ dbSNP | Ensembl ].		VAR_051877
	Natural variant	394	1	D → N. Corresponds to variant rs2336219 [ dbSNP | Ensembl ].		VAR_051878
	Natural variant	503	1	K → Q. Corresponds to variant rs3212986 [ dbSNP | Ensembl ].		VAR_051879
	Natural variant	504	1	Q → K. Ref.3 Corresponds to variant rs3212986 [ dbSNP | Ensembl ].		VAR_051880
Experimental info
	Sequence conflict	218	1	N → K in AAH54044. Ref.3
	Sequence conflict	422	1	Missing in AAI08890. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: D460FB944412D393	FASTA	510	54,986
	10 20 30 40 50 60 MEEPQAGDAA RFSCPPNFTA KPPASESPRF SLEALTGPDT ELWLIQAPAD FAPECFNGRH 70 80 90 100 110 120 VPLSGSQIVK GKLAGKRHRY RVLSSCPQAG EATLLAPSTE AGGGLTCASA PQGTLRILEG 130 140 150 160 170 180 PQQSLSGSPL QPIPASPPPQ IPPGLRPRFC AFGGNPPVTG PRSALAPNLL TSGKKKKEMQ 190 200 210 220 230 240 VTEAPVTQEA VNGHGALEVD MALGSPEMDV RKKKKKKNQQ LKEPEAAGPV GTEPTVETLE 250 260 270 280 290 300 PLGVLFPSTT KKRKKPKGKE TFEPEDKTVK QEQINTEPLE DTVLSPTKKR KRQKGTEGME 310 320 330 340 350 360 PEEGVTVESQ PQVKVEPLEE AIPLPPTKKR KKEKGQMAMM EPGTEAMEPV EPEMKPLESP 370 380 390 400 410 420 GGTMAPQQPE GAKPQAQAAL AAPKKKTKKE KQQDATVEPE TEVVGPELPD DLEPQAAPTS 430 440 450 460 470 480 TKKKKKKKER GHTVTEPIQP LEPELPGEGQ PEARATPGST KKRKKQSQES RMPETVPQEE 490 500 510 MPGPPLNSES GEEAPTGRDK KRKQQQQQPV
	Isoform 2 (CAST) [UniParc]. Checksum: 0E5BE70968A5E2C9	FASTA	512	55,172
	10 20 30 40 50 60 MEEPQAGGED AARFSCPPNF TAKPPASESP RFSLEALTGP DTELWLIQAP ADFAPECFNG 70 80 90 100 110 120 RHVPLSGSQI VKGKLAGKRH RYRVLSSCPQ AGEATLLAPS TEAGGGLTCA SAPQGTLRIL 130 140 150 160 170 180 EGPQQSLSGS PLQPIPASPP PQIPPGLRPR FCAFGGNPPV TGPRSALAPN LLTSGKKKKE 190 200 210 220 230 240 MQVTEAPVTQ EAVNGHGALE VDMALGSPEM DVRKKKKKKN QQLKEPEAAG PVGTEPTVET 250 260 270 280 290 300 LEPLGVLFPS TTKKRKKPKG KETFEPEDKT VKQEQINTEP LEDTVLSPTK KRKRQKGTEG 310 320 330 340 350 360 MEPEEGVTVE SQPQVKVEPL EEAIPLPPTK KRKKEKGQMA MMEPGTEAME PVEPEMKPLE 370 380 390 400 410 420 SPGGTMAPQQ PEGAKPQAQA ALAAPKKKTK KEKQQDATVE PETEVVGPEL PDDLEPQAAP 430 440 450 460 470 480 TSTKKKKKKK ERGHTVTEPI QPLEPELPGE GQPEARATPG STKKRKKQSQ ESRMPETVPQ 490 500 510 EEMPGPPLNS ESGEEAPTGR DKKRKQQQQQ PV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"ASE-1: a novel protein of the fibrillar centres of the nucleolus and nucleolus organizer region of mitotic chromosomes." Whitehead C.M., Winkfein R.J., Fritzler M.J., Rattner J.B. Chromosoma 106:493-502(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION. Tissue: Serum.
[2]	"CAST, a novel CD3epsilon-binding protein transducing activation signal for interleukin-2 production in T cells." Yamazaki T., Hamano Y., Tashiro H., Itoh K., Nakano H., Miyatake S., Saito T. J. Biol. Chem. 274:18173-18180(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION IN T-CELL RECEPTOR SIGNALING, PHOSPHORYLATION, INTERACTION WITH CD3E.
[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] (ISOFORM 1), VARIANT LYS-504. Tissue: Skin and Testis.
[4]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[5]	"RNA polymerase I-specific subunit CAST/hPAF49 has a role in the activation of transcription by upstream binding factor." Panov K.I., Panova T.B., Gadal O., Nishiyama K., Saito T., Russell J., Zomerdijk J.C.B.M. Mol. Cell. Biol. 26:5436-5448(2006) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE RNA POL I COMPLEX, MASS SPECTROMETRY, FUNCTION, INTERACTION WITH TAF1A AND UBTF, PHOSPHORYLATION AT TYR-80.
[6]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-309, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[7]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27; SER-128; SER-136; SER-172; SER-205; SER-285 AND THR-287, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"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-136 AND SER-490, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[9]	"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-172 AND SER-285, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-136 AND SER-285, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U86751 mRNA. Translation: AAB68608.1. AF017633 mRNA. Translation: AAD41158.1. BC038992 mRNA. Translation: AAH38992.1. BC054044 mRNA. Translation: AAH54044.1. BC108889 mRNA. Translation: AAI08890.1.
IPI	IPI00012788. IPI00645816.
RefSeq	NP_036231.1. NM_012099.1.
UniGene	Hs.710495.
3D structure databases
ProteinModelPortal	O15446.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-27616N.
IntAct	O15446. 2 interactions.
MINT	MINT-1144996.
STRING	9606.ENSP00000310966.
PTM databases
PhosphoSite	O15446.
Proteomic databases
PaxDb	O15446.
PRIDE	O15446.
Protocols and materials databases
DNASU	10849.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000309424; ENSP00000310966; ENSG00000117877. ENST00000589804; ENSP00000465099; ENSG00000117877.
GeneID	10849.
KEGG	hsa:10849.
UCSC	uc002pbq.1. human. uc002pbr.1. human.
Organism-specific databases
CTD	10849.
GeneCards	GC19P045909.
HGNC	HGNC:24219. CD3EAP.
HPA	HPA041664. HPA041734.
MIM	107325. gene.
neXtProt	NX_O15446.
PharmGKB	PA142672156.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG45026.
HOGENOM	HOG000120117.
HOVERGEN	HBG082101.
InParanoid	O15446.
OMA	FCAFGGN.
OrthoDB	EOG4NP73W.
PhylomeDB	O15446.
Gene expression databases
Bgee	O15446.
CleanEx	HS_CAST. HS_CD3EAP.
Genevestigator	O15446.
GermOnline	ENSG00000117877. Homo sapiens.
Family and domain databases
InterPro	IPR013240. DNA-dir_RNA_pol1_su_RPA34. [Graphical view]
Pfam	PF08208. RNA_polI_A34. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	CD3EAP. human.
GenomeRNAi	10849.
NextBio	41189.
SOURCE	Search...

Entry information

Entry name

RPA34_HUMAN

Accession

Primary (citable) accession number: O15446
Secondary accession number(s): Q32N11, Q7Z5U2, Q9UPF6

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 21, 2006
Last sequence update:	January 1, 1998
Last modified:	May 1, 2013
This is version 98 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.