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Q8WTR7 (ZN473_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Zinc finger protein 473
Alternative name(s):
Zinc finger protein 100 homolog
Short name=Zfp-100
Gene names
Name:ZNF473
Synonyms:KIAA1141, ZFP100
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length871 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in histone 3'-end pre-mRNA processing by associating with U7 snRNP and interacting with SLBP/pre-mRNA complex. Increases histone 3'-end pre-mRNA processing but has no effect on U7 snRNP levels, when overexpressed. Required for cell cycle progression from G1 to S phases. Ref.1 Ref.9 Ref.10

Subunit structure

Interacts with the SLBP/pre-mRNA complex but not with SLBP alone. Interacts with LSM11 in a U7 snRNP-dependent manner. Ref.1 Ref.7 Ref.8 Ref.10

Subcellular location

Nucleus. Note: Stable component of Cajal bodies (CBs). Colocalizes with SMN, coilin and U7 snRNA. Ref.10

Domain

The C2H2-type zinc finger 2 to 6 are necessary and sufficient for discrete Cajal bodies localization. The C2H2-type zinc finger 5 to 10 are necessary and sufficient for interaction with LSM11. The C2H2-type zinc finger 2 to 8 are necessary for interaction with the SLBP/RNA complex in the histone pre-mRNAs. The C2H2-type zinc finger 2 to 10 confer activity in histone pre-mRNA processing.

Sequence similarities

Belongs to the krueppel C2H2-type zinc-finger protein family.

Contains 20 C2H2-type zinc fingers.

Contains 1 KRAB domain.

Sequence caution

The sequence BAA86455.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 871871Zinc finger protein 473
PRO_0000047604

Regions

Domain6 – 7570KRAB
Zinc finger209 – 23123C2H2-type 1
Zinc finger265 – 28622C2H2-type 2; degenerate
Zinc finger320 – 34223C2H2-type 3
Zinc finger347 – 36923C2H2-type 4
Zinc finger375 – 39723C2H2-type 5
Zinc finger403 – 42523C2H2-type 6; degenerate
Zinc finger431 – 45323C2H2-type 7
Zinc finger459 – 48123C2H2-type 8
Zinc finger487 – 50923C2H2-type 9
Zinc finger515 – 53723C2H2-type 10
Zinc finger562 – 58423C2H2-type 11
Zinc finger591 – 61323C2H2-type 12
Zinc finger646 – 66823C2H2-type 13
Zinc finger674 – 69623C2H2-type 14
Zinc finger702 – 72423C2H2-type 15
Zinc finger730 – 75223C2H2-type 16
Zinc finger758 – 78023C2H2-type 17
Zinc finger786 – 80823C2H2-type 18
Zinc finger814 – 83623C2H2-type 19
Zinc finger842 – 86423C2H2-type 20
Region312 – 552241Interaction with SLBP/pre-mRNA complex

Natural variations

Natural variant591S → G.
Corresponds to variant rs10419876 [ dbSNP | Ensembl ].
VAR_052839
Natural variant741S → G.
Corresponds to variant rs10419911 [ dbSNP | Ensembl ].
VAR_052840
Natural variant1641T → M.
Corresponds to variant rs16981705 [ dbSNP | Ensembl ].
VAR_052841
Natural variant3091E → G.
Corresponds to variant rs16981706 [ dbSNP | Ensembl ].
VAR_052842
Natural variant6541T → I.
Corresponds to variant rs10424809 [ dbSNP | Ensembl ].
VAR_052843
Natural variant6621S → A.
Corresponds to variant rs10426374 [ dbSNP | Ensembl ].
VAR_052844

Experimental info

Sequence conflict4861P → A Ref.6
Sequence conflict5881V → M in BAA86455. Ref.2

Secondary structure

......................................................................................... 871
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q8WTR7 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: 959AFB7C3C2D5456

FASTA871100,182
        10         20         30         40         50         60 
MAEEFVTLKD VGMDFTLGDW EQLGLEQGDT FWDTALDNCQ DLFLLDPPRP NLTSHPDGSE 

        70         80         90        100        110        120 
DLEPLAGGSP EATSPDVTET KNSPLMEDFF EEGFSQEIIE MLSKDGFWNS NFGEACIEDT 

       130        140        150        160        170        180 
WLDSLLGDPE SLLRSDIATN GESPTECKSH ELKRGLSPVS TVSTGEDSMV HNVSEKTLTP 

       190        200        210        220        230        240 
AKSKEYRGEF FSYSDHSQQD SVQEGEKPYQ CSECGKSFSG SYRLTQHWIT HTREKPTVHQ 

       250        260        270        280        290        300 
ECEQGFDRNA SLSVYPKTHT GYKFYVCNEY GTTFSQSTYL WHQKTHTGEK PCKSQDSDHP 

       310        320        330        340        350        360 
PSHDTQPGEH QKTHTDSKSY NCNECGKAFT RIFHLTRHQK IHTRKRYECS KCQATFNLRK 

       370        380        390        400        410        420 
HLIQHQKTHA AKTTSECQEC GKIFRHSSLL IEHQALHAGE EPYKCNERGK SFRHNSTLKI 

       430        440        450        460        470        480 
HQRVHSGEKP YKCSECGKAF HRHTHLNEHR RIHTGYRPHK CQECVRSFSR PSHLMRHQAI 

       490        500        510        520        530        540 
HTAEKPYSCA ECKETFSDNN RLVQHQKMHT VKTPYECQEC GERFICGSTL KCHESVHARE 

       550        560        570        580        590        600 
KQGFFVSGKI LDQNPEQKEK CFKCNKCEKT FSCSKYLTQH ERIHTRGVKP FECDQCGKAF 

       610        620        630        640        650        660 
GQSTRLIHHQ RIHSRVRLYK WGEQGKAISS ASLIKLQSFH TKEHPFKCNE CGKTFSHSAH 

       670        680        690        700        710        720 
LSKHQLIHAG ENPFKCSKCD RVFTQRNYLV QHERTHARKK PLVCNECGKT FRQSSCLSKH 

       730        740        750        760        770        780 
QRIHSGEKPY VCDYCGKAFG LSAELVRHQR IHTGEKPYVC QECGKAFTQS SCLSIHRRVH 

       790        800        810        820        830        840 
TGEKPYRCGE CGKAFAQKAN LTQHQRIHTG EKPYSCNVCG KAFVLSAHLN QHLRVHTQET 

       850        860        870 
LYQCQRCQKA FRCHSSLSRH QRVHNKQQYC L 

« Hide

References

« Hide 'large scale' references
[1]"A novel zinc finger protein is associated with U7 snRNP and interacts with the stem-loop binding protein in the histone pre-mRNP to stimulate 3'-end processing."
Dominski Z., Erkmann J.A., Yang X., Sanchez R., Marzluff W.F.
Genes Dev. 16:58-71(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH SLBP/PRE-MRNA COMPLEX.
[2]"Characterization of cDNA clones selected by the GeneMark analysis from size-fractionated cDNA libraries from human brain."
Hirosawa M., Nagase T., Ishikawa K., Kikuno R., Nomura N., Ohara O.
DNA Res. 6:329-336(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[3]"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].
Tissue: Testis.
[4]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].
[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: Eye.
[6]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 486-871.
Tissue: Testis.
[7]"Unique Sm core structure of U7 snRNPs: assembly by a specialized SMN complex and the role of a new component, Lsm11, in histone RNA processing."
Pillai R.S., Grimmler M., Meister G., Will C.L., Luehrmann R., Fischer U., Schuemperli D.
Genes Dev. 17:2321-2333(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH LSM11.
Tissue: Cervix carcinoma.
[8]"U7 snRNP-specific Lsm11 protein: dual binding contacts with the 100 kDa zinc finger processing factor (ZFP100) and a ZFP100-independent function in histone RNA 3'-end processing."
Azzouz T.N., Gruber A., Schuemperli D.
Nucleic Acids Res. 33:2106-2117(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH LSM11.
[9]"ZFP100, a component of the active U7 snRNP limiting for histone pre-mRNA processing, is required for entry into S phase."
Wagner E.J., Marzluff W.F.
Mol. Cell. Biol. 26:6702-6712(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[10]"Conserved zinc fingers mediate multiple functions of ZFP100, a U7snRNP associated protein."
Wagner E.J., Ospina J.K., Hu Y., Dundr M., Matera A.G., Marzluff W.F.
RNA 12:1206-1218(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH LSM11, SUBCELLULAR LOCATION.
[11]"Solution structure of the C2H2 type zinc finger region of human zinc finger protein 473."
RIKEN structural genomics initiative (RSGI)
Submitted (OCT-2007) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 205-841.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF454744 mRNA. Translation: AAL51029.1.
AB032967 mRNA. Translation: BAA86455.1. Different initiation.
AK292452 mRNA. Translation: BAF85141.1.
CH471177 Genomic DNA. Translation: EAW52593.1.
BC018612 mRNA. Translation: AAH18612.1.
AL080143 mRNA. Translation: CAB45736.1.
CCDSCCDS33077.1.
PIRT12527.
RefSeqNP_001006657.1. NM_001006656.1.
NP_056243.1. NM_015428.1.
UniGeneHs.440553.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2EMBNMR-A342-372[»]
2EMCNMR-A641-673[»]
2EMENMR-A725-757[»]
2EOUNMR-A370-400[»]
2EOXNMR-A315-345[»]
2EOYNMR-A557-589[»]
2EOZNMR-A809-841[»]
2YRHNMR-A699-729[»]
2YRJNMR-A781-813[»]
2YSVNMR-A755-783[»]
2YTDNMR-A426-458[»]
2YTENMR-A484-512[»]
2YTTNMR-A204-236[»]
2YU5NMR-A669-699[»]
ProteinModelPortalQ8WTR7.
SMRQ8WTR7. Positions 171-867.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117398. 7 interactions.
IntActQ8WTR7. 4 interactions.
MINTMINT-1441474.
STRING9606.ENSP00000270617.

PTM databases

PhosphoSiteQ8WTR7.

Polymorphism databases

DMDM51702187.

Proteomic databases

PaxDbQ8WTR7.
PRIDEQ8WTR7.

Protocols and materials databases

DNASU25888.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000270617; ENSP00000270617; ENSG00000142528.
ENST00000391821; ENSP00000375697; ENSG00000142528.
ENST00000595661; ENSP00000472808; ENSG00000142528.
GeneID25888.
KEGGhsa:25888.
UCSCuc002prm.3. human.

Organism-specific databases

CTD25888.
GeneCardsGC19P050529.
HGNCHGNC:23239. ZNF473.
HPAHPA004191.
neXtProtNX_Q8WTR7.
PharmGKBPA134987987.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5048.
HOGENOMHOG000234617.
HOVERGENHBG018163.
InParanoidQ8WTR7.
KOK09228.
OMACAECKET.
OrthoDBEOG7KSX7Q.
PhylomeDBQ8WTR7.
TreeFamTF350932.

Enzyme and pathway databases

ReactomeREACT_1788. Transcription.
REACT_71. Gene Expression.
REACT_78. Post-Elongation Processing of the Transcript.

Gene expression databases

ArrayExpressQ8WTR7.
BgeeQ8WTR7.
CleanExHS_ZNF473.
GenevestigatorQ8WTR7.

Family and domain databases

Gene3D3.30.160.60. 21 hits.
InterProIPR001909. Krueppel-associated_box.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
PfamPF01352. KRAB. 1 hit.
PF00096. zf-C2H2. 3 hits.
[Graphical view]
SMARTSM00349. KRAB. 1 hit.
SM00355. ZnF_C2H2. 20 hits.
[Graphical view]
SUPFAMSSF109640. SSF109640. 1 hit.
PROSITEPS50805. KRAB. 1 hit.
PS00028. ZINC_FINGER_C2H2_1. 18 hits.
PS50157. ZINC_FINGER_C2H2_2. 20 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ8WTR7.
GeneWikiZNF473.
GenomeRNAi25888.
NextBio47312.
PROQ8WTR7.

Entry information

Entry nameZN473_HUMAN
AccessionPrimary (citable) accession number: Q8WTR7
Secondary accession number(s): A8K8T7, Q9ULS9, Q9Y4Q7
Entry history
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: March 1, 2002
Last modified: July 9, 2014
This is version 110 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM