Q8WTR7 (ZN473_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Zinc finger protein 473

Alternative name(s):
Zinc finger protein 100 homolog
Short name=Zfp-100

Gene names

Name:	ZNF473
Synonyms:	KIAA1141, ZFP100

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	871 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Cellular component	Nucleus
Coding sequence diversity	Polymorphism
Domain	Repeat Zinc-finger
Ligand	DNA-binding Metal-binding Zinc
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	histone mRNA 3'-end processing Inferred from direct assay Ref.10. Source: UniProtKB regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: InterPro termination of RNA polymerase II transcription Traceable author statement. Source: Reactome
Cellular_component	Cajal body Inferred from direct assay Ref.10. Source: UniProtKB
Molecular_function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 871

871

Zinc finger protein 473

PRO_0000047604

Regions

Domain

6 – 75

70

KRAB

Zinc finger

209 – 231

23

C2H2-type 1

Zinc finger

265 – 286

22

C2H2-type 2; degenerate

Zinc finger

320 – 342

23

C2H2-type 3

Zinc finger

347 – 369

23

C2H2-type 4

Zinc finger

375 – 397

23

C2H2-type 5

Zinc finger

403 – 425

23

C2H2-type 6; degenerate

Zinc finger

431 – 453

23

C2H2-type 7

Zinc finger

459 – 481

23

C2H2-type 8

Zinc finger

487 – 509

23

C2H2-type 9

Zinc finger

515 – 537

23

C2H2-type 10

Zinc finger

562 – 584

23

C2H2-type 11

Zinc finger

591 – 613

23

C2H2-type 12

Zinc finger

646 – 668

23

C2H2-type 13

Zinc finger

674 – 696

23

C2H2-type 14

Zinc finger

702 – 724

23

C2H2-type 15

Zinc finger

730 – 752

23

C2H2-type 16

Zinc finger

758 – 780

23

C2H2-type 17

Zinc finger

786 – 808

23

C2H2-type 18

Zinc finger

814 – 836

23

C2H2-type 19

Zinc finger

842 – 864

23

C2H2-type 20

Region

312 – 552

241

Interaction with SLBP/pre-mRNA complex

Natural variations

Natural variant

59

1

S → G.
Corresponds to variant rs10419876 [ dbSNP | Ensembl ].

VAR_052839

Natural variant

74

1

S → G.
Corresponds to variant rs10419911 [ dbSNP | Ensembl ].

VAR_052840

Natural variant

164

1

T → M.
Corresponds to variant rs16981705 [ dbSNP | Ensembl ].

VAR_052841

Natural variant

309

1

E → G.
Corresponds to variant rs16981706 [ dbSNP | Ensembl ].

VAR_052842

Natural variant

654

1

T → I.
Corresponds to variant rs10424809 [ dbSNP | Ensembl ].

VAR_052843

Natural variant

662

1

S → A.
Corresponds to variant rs10426374 [ dbSNP | Ensembl ].

VAR_052844

Experimental info

Sequence conflict

486

1

P → A Ref.6

Sequence conflict

588

1

V → M in BAA86455. Ref.2

Secondary structure

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871

Helix Strand Turn

Details...

Beta strand

212 – 214

3

Helix

221 – 228

8

Helix

230 – 233

4

Beta strand

320 – 322

3

Turn

323 – 326

4

Beta strand

327 – 332

6

Helix

333 – 336

4

Helix

339 – 342

4

Beta strand

345 – 348

4

Turn

350 – 352

3

Beta strand

355 – 357

3

Helix

359 – 365

7

Helix

366 – 369

4

Beta strand

370 – 372

3

Turn

378 – 380

3

Helix

387 – 397

11

Beta strand

430 – 432

3

Beta strand

434 – 436

3

Beta strand

439 – 442

4

Helix

443 – 453

11

Turn

490 – 492

3

Helix

499 – 508

10

Beta strand

565 – 567

3

Beta strand

570 – 574

5

Helix

575 – 581

7

Beta strand

645 – 647

3

Beta strand

649 – 651

3

Beta strand

654 – 657

4

Helix

658 – 665

8

Turn

666 – 670

5

Beta strand

673 – 675

3

Beta strand

677 – 680

4

Beta strand

682 – 686

5

Helix

687 – 695

9

Turn

705 – 707

3

Beta strand

710 – 713

4

Helix

714 – 721

8

Turn

722 – 724

3

Beta strand

729 – 731

3

Beta strand

733 – 735

3

Beta strand

738 – 741

4

Helix

742 – 749

8

Helix

750 – 752

3

Beta strand

761 – 763

3

Beta strand

768 – 771

4

Helix

772 – 778

7

Beta strand

789 – 791

3

Beta strand

794 – 797

4

Helix

798 – 805

8

Turn

806 – 808

3

Beta strand

813 – 816

4

Turn

817 – 820

4

Beta strand

821 – 825

5

Helix

826 – 836

11

Sequences

	Sequence		Length	Mass (Da)
	Q8WTR7 [UniParc]. Last modified March 1, 2002. Version 1. Checksum: 959AFB7C3C2D5456	FASTA	871	100,182
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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.

IPI

IPI00297388.

PIR

T12527.

RefSeq

NP_001006657.1. NM_001006656.1.
NP_056243.1. NM_015428.1.

UniGene

Hs.440553.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2EMB	NMR	-	A	342-372	[»]
2EMC	NMR	-	A	641-673	[»]
2EME	NMR	-	A	725-757	[»]
2EOU	NMR	-	A	370-400	[»]
2EOX	NMR	-	A	315-345	[»]
2EOY	NMR	-	A	557-589	[»]
2EOZ	NMR	-	A	809-841	[»]
2YRH	NMR	-	A	699-729	[»]
2YRJ	NMR	-	A	781-813	[»]
2YSV	NMR	-	A	755-783	[»]
2YTD	NMR	-	A	426-458	[»]
2YTE	NMR	-	A	484-512	[»]
2YTT	NMR	-	A	204-236	[»]
2YU5	NMR	-	A	669-699	[»]

ProteinModelPortal

Q8WTR7.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q8WTR7. 4 interactions.

MINT

MINT-1441474.

STRING

9606.ENSP00000270617.

PTM databases

PhosphoSite

Q8WTR7.

Polymorphism databases

DMDM

51702187.

Proteomic databases

PaxDb

Q8WTR7.

PRIDE

Q8WTR7.

Protocols and materials databases

DNASU

25888.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000270617; ENSP00000270617; ENSG00000142528.
ENST00000391821; ENSP00000375697; ENSG00000142528.
ENST00000595661; ENSP00000472808; ENSG00000142528.

GeneID

25888.

KEGG

hsa:25888.

UCSC

uc002prm.3. human.

Organism-specific databases

CTD

25888.

GeneCards

GC19P050529.

HGNC

HGNC:23239. ZNF473.

HPA

HPA004191.

neXtProt

NX_Q8WTR7.

PharmGKB

PA134987987.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5048.

HOGENOM

HOG000234617.

HOVERGEN

HBG018163.

InParanoid

Q8WTR7.

KO

K09228.

OMA

CAECKET.

OrthoDB

EOG4C5CHP.

Enzyme and pathway databases

Reactome

REACT_1675. mRNA Processing.
REACT_1788. Transcription.
REACT_71. Gene Expression.
REACT_78. Post-Elongation Processing of the Transcript.

Gene expression databases

ArrayExpress

Q8WTR7.

Bgee

Q8WTR7.

CleanEx

HS_ZNF473.

Genevestigator

Q8WTR7.

GermOnline

ENSG00000142528. Homo sapiens.

Family and domain databases

Gene3D

3.30.160.60. 21 hits.

InterPro

IPR001909. Krueppel-associated_box.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]

Pfam

PF01352. KRAB. 1 hit.
PF00096. zf-C2H2. 3 hits.
[Graphical view]

SMART

SM00349. KRAB. 1 hit.
SM00355. ZnF_C2H2. 20 hits.
[Graphical view]

SUPFAM

SSF109640. Krueppel-associated_box. 1 hit.

PROSITE

PS50805. KRAB. 1 hit.
PS00028. ZINC_FINGER_C2H2_1. 18 hits.
PS50157. ZINC_FINGER_C2H2_2. 20 hits.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q8WTR7.

GenomeRNAi

25888.

NextBio

47312.

Entry information

Entry name

ZN473_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 101 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.