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Protein

DNA-directed RNA polymerase I subunit RPA12

Gene

ZNRD1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

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.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri20 – 4122C4-typeSequence analysisAdd
BLAST
Zinc fingeri83 – 12341TFIIS-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Transcription

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-HSA-427413. NoRC negatively regulates rRNA expression.
R-HSA-5250924. B-WICH complex positively regulates rRNA expression.
R-HSA-73762. RNA Polymerase I Transcription Initiation.
R-HSA-73772. RNA Polymerase I Promoter Escape.
R-HSA-73777. RNA Polymerase I Chain Elongation.
R-HSA-73863. RNA Polymerase I Transcription Termination.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA-directed RNA polymerase I subunit RPA12
Alternative name(s):
Zinc ribbon domain-containing protein 1
Gene namesi
Name:ZNRD1
Synonyms:RPA12
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:13182. ZNRD1.

Subcellular locationi

  • Nucleusnucleolus By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

DNA-directed RNA polymerase, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA37754.

Polymorphism and mutation databases

DMDMi71649339.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 126126DNA-directed RNA polymerase I subunit RPA12PRO_0000121460Add
BLAST

Proteomic databases

EPDiQ9P1U0.
MaxQBiQ9P1U0.
PaxDbiQ9P1U0.
PeptideAtlasiQ9P1U0.
PRIDEiQ9P1U0.

Expressioni

Gene expression databases

BgeeiQ9P1U0.
CleanExiHS_ZNRD1.
ExpressionAtlasiQ9P1U0. baseline and differential.
GenevisibleiQ9P1U0. HS.

Interactioni

Subunit structurei

Component of the RNA polymerase I (Pol I) complex consisting of at least 13 subunits.By similarity

Protein-protein interaction databases

BioGridi119050. 22 interactions.
IntActiQ9P1U0. 18 interactions.
MINTiMINT-1435192.
STRINGi9606.ENSP00000331111.

Structurei

3D structure databases

ProteinModelPortaliQ9P1U0.
SMRiQ9P1U0. Positions 12-121.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Contains 1 TFIIS-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri20 – 4122C4-typeSequence analysisAdd
BLAST
Zinc fingeri83 – 12341TFIIS-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG2907. Eukaryota.
COG1594. LUCA.
GeneTreeiENSGT00390000008126.
HOGENOMiHOG000228133.
HOVERGENiHBG055084.
InParanoidiQ9P1U0.
KOiK03000.
OMAiFFTCIHC.
OrthoDBiEOG7HMS3G.
PhylomeDBiQ9P1U0.
TreeFamiTF313881.

Family and domain databases

InterProiIPR019761. DNA-dir_RNA_pol-M_15_CS.
IPR012164. Rpa12/Rpb9/Rpc10/TFS.
IPR001222. Znf_TFIIS.
[Graphical view]
PfamiPF01096. TFIIS_C. 1 hit.
[Graphical view]
PIRSFiPIRSF005586. RNApol_RpoM. 1 hit.
SMARTiSM00440. ZnF_C2C2. 1 hit.
[Graphical view]
PROSITEiPS01030. RNA_POL_M_15KD. 1 hit.
PS00466. ZF_TFIIS_1. 1 hit.
PS51133. ZF_TFIIS_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9P1U0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSVMDLANTC SSFQSDLDFC SDCGSVLPLP GAQDTVTCIR CGFNINVRDF
60 70 80 90 100
EGKVVKTSVV FHQLGTAMPM SVEEGPECQG PVVDRRCPRC GHEGMAYHTR
110 120
QMRSADEGQT VFYTCTNCKF QEKEDS
Length:126
Mass (Da):13,904
Last modified:October 1, 2000 - v1
Checksum:iC678AC7132A91432
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti14 – 141Q → H.
Corresponds to variant rs17187658 [ dbSNP | Ensembl ].
VAR_052287

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF024617 mRNA. Translation: AAF40469.1.
AF230337 mRNA. Translation: AAG50159.1.
AF230338 Genomic DNA. Translation: AAG50160.1.
CR457109 mRNA. Translation: CAG33390.1.
AL669914 Genomic DNA. Translation: CAI18176.1.
AL671859 Genomic DNA. Translation: CAI17577.1.
AL845439 Genomic DNA. Translation: CAI18538.1.
BX088647 Genomic DNA. Translation: CAI95579.1.
BC010898 mRNA. Translation: AAH10898.1.
BC050608 mRNA. Translation: AAH50608.1.
CCDSiCCDS4670.1.
RefSeqiNP_001265714.1. NM_001278785.1.
NP_001265715.1. NM_001278786.1.
NP_055411.1. NM_014596.5.
NP_740753.1. NM_170783.3.
UniGeneiHs.57813.

Genome annotation databases

EnsembliENST00000332435; ENSP00000331111; ENSG00000066379.
ENST00000359374; ENSP00000352333; ENSG00000066379.
ENST00000376782; ENSP00000365978; ENSG00000066379.
ENST00000376785; ENSP00000365981; ENSG00000066379.
ENST00000383613; ENSP00000373108; ENSG00000206502.
ENST00000400659; ENSP00000383500; ENSG00000206502.
ENST00000400660; ENSP00000383501; ENSG00000206502.
ENST00000400662; ENSP00000383503; ENSG00000206502.
ENST00000412396; ENSP00000396922; ENSG00000233795.
ENST00000417275; ENSP00000397636; ENSG00000233795.
ENST00000417738; ENSP00000407715; ENSG00000235176.
ENST00000420100; ENSP00000410530; ENSG00000236808.
ENST00000428913; ENSP00000414110; ENSG00000224859.
ENST00000429558; ENSP00000410954; ENSG00000235176.
ENST00000431032; ENSP00000416599; ENSG00000236949.
ENST00000431416; ENSP00000395065; ENSG00000235176.
ENST00000432227; ENSP00000399302; ENSG00000236808.
ENST00000432545; ENSP00000405264; ENSG00000236949.
ENST00000432904; ENSP00000414720; ENSG00000236808.
ENST00000433264; ENSP00000393236; ENSG00000236949.
ENST00000437373; ENSP00000410127; ENSG00000236949.
ENST00000437507; ENSP00000412369; ENSG00000235443.
ENST00000441251; ENSP00000413265; ENSG00000235176.
ENST00000442585; ENSP00000394779; ENSG00000233795.
ENST00000443142; ENSP00000391809; ENSG00000235443.
ENST00000443494; ENSP00000395397; ENSG00000235443.
ENST00000444027; ENSP00000396661; ENSG00000236808.
ENST00000444794; ENSP00000407364; ENSG00000233795.
ENST00000446493; ENSP00000399966; ENSG00000224859.
ENST00000451875; ENSP00000387914; ENSG00000224859.
ENST00000453694; ENSP00000405636; ENSG00000235443.
ENST00000455948; ENSP00000402198; ENSG00000224859.
GeneIDi30834.
KEGGihsa:30834.
UCSCiuc003noz.5. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF024617 mRNA. Translation: AAF40469.1.
AF230337 mRNA. Translation: AAG50159.1.
AF230338 Genomic DNA. Translation: AAG50160.1.
CR457109 mRNA. Translation: CAG33390.1.
AL669914 Genomic DNA. Translation: CAI18176.1.
AL671859 Genomic DNA. Translation: CAI17577.1.
AL845439 Genomic DNA. Translation: CAI18538.1.
BX088647 Genomic DNA. Translation: CAI95579.1.
BC010898 mRNA. Translation: AAH10898.1.
BC050608 mRNA. Translation: AAH50608.1.
CCDSiCCDS4670.1.
RefSeqiNP_001265714.1. NM_001278785.1.
NP_001265715.1. NM_001278786.1.
NP_055411.1. NM_014596.5.
NP_740753.1. NM_170783.3.
UniGeneiHs.57813.

3D structure databases

ProteinModelPortaliQ9P1U0.
SMRiQ9P1U0. Positions 12-121.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119050. 22 interactions.
IntActiQ9P1U0. 18 interactions.
MINTiMINT-1435192.
STRINGi9606.ENSP00000331111.

Polymorphism and mutation databases

DMDMi71649339.

Proteomic databases

EPDiQ9P1U0.
MaxQBiQ9P1U0.
PaxDbiQ9P1U0.
PeptideAtlasiQ9P1U0.
PRIDEiQ9P1U0.

Protocols and materials databases

DNASUi30834.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000332435; ENSP00000331111; ENSG00000066379.
ENST00000359374; ENSP00000352333; ENSG00000066379.
ENST00000376782; ENSP00000365978; ENSG00000066379.
ENST00000376785; ENSP00000365981; ENSG00000066379.
ENST00000383613; ENSP00000373108; ENSG00000206502.
ENST00000400659; ENSP00000383500; ENSG00000206502.
ENST00000400660; ENSP00000383501; ENSG00000206502.
ENST00000400662; ENSP00000383503; ENSG00000206502.
ENST00000412396; ENSP00000396922; ENSG00000233795.
ENST00000417275; ENSP00000397636; ENSG00000233795.
ENST00000417738; ENSP00000407715; ENSG00000235176.
ENST00000420100; ENSP00000410530; ENSG00000236808.
ENST00000428913; ENSP00000414110; ENSG00000224859.
ENST00000429558; ENSP00000410954; ENSG00000235176.
ENST00000431032; ENSP00000416599; ENSG00000236949.
ENST00000431416; ENSP00000395065; ENSG00000235176.
ENST00000432227; ENSP00000399302; ENSG00000236808.
ENST00000432545; ENSP00000405264; ENSG00000236949.
ENST00000432904; ENSP00000414720; ENSG00000236808.
ENST00000433264; ENSP00000393236; ENSG00000236949.
ENST00000437373; ENSP00000410127; ENSG00000236949.
ENST00000437507; ENSP00000412369; ENSG00000235443.
ENST00000441251; ENSP00000413265; ENSG00000235176.
ENST00000442585; ENSP00000394779; ENSG00000233795.
ENST00000443142; ENSP00000391809; ENSG00000235443.
ENST00000443494; ENSP00000395397; ENSG00000235443.
ENST00000444027; ENSP00000396661; ENSG00000236808.
ENST00000444794; ENSP00000407364; ENSG00000233795.
ENST00000446493; ENSP00000399966; ENSG00000224859.
ENST00000451875; ENSP00000387914; ENSG00000224859.
ENST00000453694; ENSP00000405636; ENSG00000235443.
ENST00000455948; ENSP00000402198; ENSG00000224859.
GeneIDi30834.
KEGGihsa:30834.
UCSCiuc003noz.5. human.

Organism-specific databases

CTDi30834.
GeneCardsiZNRD1.
HGNCiHGNC:13182. ZNRD1.
MIMi607525. gene.
neXtProtiNX_Q9P1U0.
PharmGKBiPA37754.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2907. Eukaryota.
COG1594. LUCA.
GeneTreeiENSGT00390000008126.
HOGENOMiHOG000228133.
HOVERGENiHBG055084.
InParanoidiQ9P1U0.
KOiK03000.
OMAiFFTCIHC.
OrthoDBiEOG7HMS3G.
PhylomeDBiQ9P1U0.
TreeFamiTF313881.

Enzyme and pathway databases

ReactomeiR-HSA-427413. NoRC negatively regulates rRNA expression.
R-HSA-5250924. B-WICH complex positively regulates rRNA expression.
R-HSA-73762. RNA Polymerase I Transcription Initiation.
R-HSA-73772. RNA Polymerase I Promoter Escape.
R-HSA-73777. RNA Polymerase I Chain Elongation.
R-HSA-73863. RNA Polymerase I Transcription Termination.

Miscellaneous databases

GeneWikiiZNRD1.
GenomeRNAii30834.
PROiQ9P1U0.
SOURCEiSearch...

Gene expression databases

BgeeiQ9P1U0.
CleanExiHS_ZNRD1.
ExpressionAtlasiQ9P1U0. baseline and differential.
GenevisibleiQ9P1U0. HS.

Family and domain databases

InterProiIPR019761. DNA-dir_RNA_pol-M_15_CS.
IPR012164. Rpa12/Rpb9/Rpc10/TFS.
IPR001222. Znf_TFIIS.
[Graphical view]
PfamiPF01096. TFIIS_C. 1 hit.
[Graphical view]
PIRSFiPIRSF005586. RNApol_RpoM. 1 hit.
SMARTiSM00440. ZnF_C2C2. 1 hit.
[Graphical view]
PROSITEiPS01030. RNA_POL_M_15KD. 1 hit.
PS00466. ZF_TFIIS_1. 1 hit.
PS51133. ZF_TFIIS_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A new zinc ribbon gene (ZNRD1) is cloned from the human MHC class I region."
    Fan W., Wang Z., Kyzysztof F., Prange C., Lennon G.
    Genomics 63:139-141(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Complementation studies of Rpa12, small specific subunit of nuclear RNA polymerase I."
    Shematorova E.K., Lebedenko E.N., Shpakovski G.V.
    Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
  3. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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].
    Tissue: Skeletal muscle and Skin.

Entry informationi

Entry nameiRPA12_HUMAN
AccessioniPrimary (citable) accession number: Q9P1U0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 2, 2005
Last sequence update: October 1, 2000
Last modified: June 8, 2016
This is version 131 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.