A2A288 (ZC12D_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Probable ribonuclease ZC3H12D
EC=3.1.-.-

Alternative name(s):
MCP-induced protein 4
Transformed follicular lymphoma
Zinc finger CCCH domain-containing protein 12D
p34

Gene names

Name:	ZC3H12D
Synonyms:	C6orf95, MCPIP4, TFL

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	527 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	May regulate cell growth likely by suppressing RB1 phosphorylation. May function as RNase and regulate the levels of target RNA species Potential. Serve as a tumor suppressor in certain leukemia cells. Overexpression inhibits the G1 to S phase progression through suppression of RB1 phosphorylation. Ref.1 Ref.6
Cofactor	Magnesium Potential.
Subcellular location	Isoform 1: Cytoplasm. Note: Localized as discrete granules. Colocalized with mRNA-processing body markers, EIF2C2 and DCP1A, but not with a stress granule maker, TIA1, in the cytoplasm. Ref.1 Isoform 3: Cytoplasm. Nucleus Ref.1.
Tissue specificity	Expressed in normal human lymphocytes but defective in some leukemia/lymphoma cell lines. Ref.1
Induction	By prolonged exposure to bacterial lipopolysaccharides (LPS) in acute monocytic leukemia cell line THP-1 cells. Ref.7
Involvement in disease	A chromosomal aberration involving ZC3H12D may be the cause of the transformation of follicular lymphoma (FL) to diffuse large B-cell lymphoma (DLBCL). Translocation t(2;6)(p12;q25) with IGK. Resulting protein may not be expressed.
Sequence similarities	Belongs to the ZC3H12 family. UniProtKB A6QQJ8 Contains 1 C3H1-type zinc finger. UniProtKB A6QQJ8

Ontologies

Keywords
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing Chromosomal rearrangement Polymorphism
Domain	Zinc-finger
Ligand	Magnesium Metal-binding Zinc
Molecular function	Endonuclease Hydrolase Nuclease
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	negative regulation of G1/S transition of mitotic cell cycle Inferred from direct assay Ref.1. Source: UniProtKB negative regulation of cell growth Inferred from direct assay Ref.1. Source: UniProtKB nucleic acid phosphodiester bond hydrolysis Inferred from electronic annotation. Source: GOC
Cellular_component	cytoplasm Inferred from direct assay Ref.1. Source: UniProtKB nucleus Inferred from direct assay. Source: HPA
Molecular_function	endonuclease activity Inferred from electronic annotation. Source: UniProtKB-KW nucleic acid binding Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 Ref.3 (identifier: A2A288-1)

Also known as: P58TFL; TFL1;

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 Ref.3 (identifier: A2A288-3)

The sequence of this isoform differs from the canonical sequence as follows:
     228-527: Missing.

Note: No experimental confirmation available.

Isoform 3 Ref.4 (identifier: A2A288-4)

Also known as: P36TFL; TFL2;

The sequence of this isoform differs from the canonical sequence as follows:
     300-321: GAGAEEQRPPRAPGGSAGARAA → VLPGRPPASARPAAPAAGRTPP
     322-527: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 527	527	Probable ribonuclease ZC3H12D		PRO_0000348931
Regions
	Zinc finger	248 – 279	32	C3H1-type
	Compositional bias	357 – 441	85	Pro-rich
Natural variations
	Alternative sequence	228 – 527	300	Missing in isoform 2. Ref.4		VSP_052853
	Alternative sequence	300 – 321	22	GAGAE…GARAA → VLPGRPPASARPAAPAAGRT PP in isoform 3.		VSP_040794
	Alternative sequence	322 – 527	206	Missing in isoform 3. Ref.3		VSP_040795
	Natural variant	53	1	P → L. Ref.1 Ref.2 Ref.3 Corresponds to variant rs7747948 [ dbSNP | Ensembl ].		VAR_046199
	Natural variant	106	1	K → R in some sporadic lung cancer sample; appears to cause loss of tumor suppressor activity. Ref.6 Corresponds to variant rs61997220 [ dbSNP | Ensembl ].		VAR_046200
Experimental info
	Sequence conflict	135	1	S → F in BAH28269. Ref.1
	Sequence conflict	140	1	P → S in BAH28269. Ref.1
	Sequence conflict	140	1	P → S in BAC87196. Ref.2
	Sequence conflict	299	1	P → L in BAH28269. Ref.1
	Sequence conflict	299	1	P → L in BAC87196. Ref.2
	Sequence conflict	405	1	P → S in AAI57833. Ref.4
	Sequence conflict	499	1	A → T in AAI57833. Ref.4
Isoform 3:
	Sequence conflict	300	1	V → G in BAH28269. Ref.1
	Sequence conflict	301	1	L → V in BAH28269. Ref.1
	Sequence conflict	302	1	P → R in BAH28269. Ref.1
	Sequence conflict	300	1	V → G in BAC87196. Ref.2
	Sequence conflict	301	1	L → V in BAC87196. Ref.2
	Sequence conflict	302	1	P → R in BAC87196. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (P58TFL) (TFL1) [UniParc]. Last modified September 1, 2009. Version 3. Checksum: E330D92548D49DD7	FASTA	527	58,078
	10 20 30 40 50 60 MEHPSKMEFF QKLGYDREDV LRVLGKLGEG ALVNDVLQEL IRTGSRPGAL EHPAAPRLVP 70 80 90 100 110 120 RGSCGVPDSA QRGPGTALEE DFRTLASSLR PIVIDGSNVA MSHGNKETFS CRGIKLAVDW 130 140 150 160 170 180 FRDRGHTYIK VFVPSWRKDP PRADTPIREQ HVLAELERQA VLVYTPSRKV HGKRLVCYDD 190 200 210 220 230 240 RYIVKVAYEQ DGVIVSNDNY RDLQSENPEW KWFIEQRLLM FSFVNDRFMP PDDPLGRHGP 250 260 270 280 290 300 SLSNFLSRKP KPPEPSWQHC PYGKKCTYGI KCKFYHPERP HHAQLAVADE LRAKTGARPG 310 320 330 340 350 360 AGAEEQRPPR APGGSAGARA APREPFAHSL PPARGSPDLA ALRGSFSRLA FSDDLGPLGP 370 380 390 400 410 420 PLPVPACSLT PRLGGPDWVS AGGRVPGPLS LPSPESQFSP GDLPPPPGLQ LQPRGEHRPR 430 440 450 460 470 480 DLHGDLLSPR RPPDDPWARP PRSDRFPGRS VWAEPAWGDG ATGGLSVYAT EDDEGDARAR 490 500 510 520 ARIALYSVFP RDQVDRVMAA FPELSDLARL ILLVQRCQSA GAPLGKP
	Isoform 2 [UniParc]. Checksum: 5267FCB7B992C467	FASTA	227	25,951
	10 20 30 40 50 60 MEHPSKMEFF QKLGYDREDV LRVLGKLGEG ALVNDVLQEL IRTGSRPGAL EHPAAPRLVP 70 80 90 100 110 120 RGSCGVPDSA QRGPGTALEE DFRTLASSLR PIVIDGSNVA MSHGNKETFS CRGIKLAVDW 130 140 150 160 170 180 FRDRGHTYIK VFVPSWRKDP PRADTPIREQ HVLAELERQA VLVYTPSRKV HGKRLVCYDD 190 200 210 220 RYIVKVAYEQ DGVIVSNDNY RDLQSENPEW KWFIEQRLLM FSFVNDR
	Isoform 3 (P36TFL) (TFL2) [UniParc]. Checksum: 268B27A7F6375628	FASTA	321	36,199
	10 20 30 40 50 60 MEHPSKMEFF QKLGYDREDV LRVLGKLGEG ALVNDVLQEL IRTGSRPGAL EHPAAPRLVP 70 80 90 100 110 120 RGSCGVPDSA QRGPGTALEE DFRTLASSLR PIVIDGSNVA MSHGNKETFS CRGIKLAVDW 130 140 150 160 170 180 FRDRGHTYIK VFVPSWRKDP PRADTPIREQ HVLAELERQA VLVYTPSRKV HGKRLVCYDD 190 200 210 220 230 240 RYIVKVAYEQ DGVIVSNDNY RDLQSENPEW KWFIEQRLLM FSFVNDRFMP PDDPLGRHGP 250 260 270 280 290 300 SLSNFLSRKP KPPEPSWQHC PYGKKCTYGI KCKFYHPERP HHAQLAVADE LRAKTGARPV 310 320 LPGRPPASAR PAAPAAGRTP P

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Inhibition of G(1) to S phase progression by a novel zinc finger protein P58(TFL) at P-bodies." Minagawa K., Katayama Y., Nishikawa S., Yamamoto K., Sada A., Okamura A., Shimoyama M., Matsui T. Mol. Cancer Res. 7:880-889(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, VARIANT LEU-53.
[2]	"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] (ISOFORM 3), VARIANT LEU-53. Tissue: Spleen.
[3]	"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].
[4]	"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] (ISOFORMS 1 AND 2). Tissue: Brain cortex.
[5]	"Deregulation of a possible tumour suppressor gene, ZC3H12D, by translocation of IGK@ in transformed follicular lymphoma with t(2;6)(p12;q25)." Minagawa K., Yamamoto K., Nishikawa S., Ito M., Sada A., Yakushijin K., Okamura A., Shimoyama M., Katayama Y., Matsui T. Br. J. Haematol. 139:161-163(2007) [PubMed] [Europe PMC] [Abstract] Cited for: CHROMOSOMAL TRANSLOCATION, INVOLVEMENT IN DIFFUSE LARGE B-CELL LYMPHOMA.
[6]	"Identification of a novel tumor suppressor gene p34 on human chromosome 6q25.1." Wang M., Vikis H.G., Wang Y., Jia D., Wang D., Bierut L.J., Bailey-Wilson J.E., Amos C.I., Pinney S.M., Petersen G.M., de Andrade M., Yang P., Wiest J.S., Fain P.R., Schwartz A.G., Gazdar A., Minna J., Gaba C. , Rothschild H., Mandal D., Kupert E., Seminara D., Liu Y., Viswanathan A., Govindan R., Anderson M.W., You M. Cancer Res. 67:93-99(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, VARIANT ARG-106.
[7]	"A novel CCCH-zinc finger protein family regulates proinflammatory activation of macrophages." Liang J., Wang J., Azfer A., Song W., Tromp G., Kolattukudy P.E., Fu M. J. Biol. Chem. 283:6337-6346(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INDUCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB458221 mRNA. Translation: BAH28268.1. AB458222 mRNA. Translation: BAH28269.1. AK127932 mRNA. Translation: BAC87196.1. AL031133 Genomic DNA. Translation: CAM28211.2. BC127762 mRNA. Translation: AAI27763.1. BC157832 mRNA. Translation: AAI57833.1.
IPI	IPI00854887. IPI00943634. IPI01009660.
RefSeq	NP_997243.2. NM_207360.2.
UniGene	Hs.632618.
3D structure databases
ProteinModelPortal	A2A288.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000374592.
PTM databases
PhosphoSite	A2A288.
Proteomic databases
PaxDb	A2A288.
PRIDE	A2A288.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000389942; ENSP00000374592; ENSG00000178199. ENST00000409806; ENSP00000386616; ENSG00000178199. ENST00000542614; ENSP00000440813; ENSG00000178199.
GeneID	340152.
KEGG	hsa:340152.
UCSC	uc003qmn.1. human. uc010kid.3. human.
Organism-specific databases
CTD	340152.
GeneCards	GC06M149811.
HGNC	HGNC:21175. ZC3H12D.
HPA	HPA036897.
MIM	611106. gene.
neXtProt	NX_A2A288.
PharmGKB	PA134867170.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG259385.
HOGENOM	HOG000060218.
HOVERGEN	HBG108759.
InParanoid	A2A288.
OMA	WAEPAWG.
OrthoDB	EOG4CRKZW.
Gene expression databases
ArrayExpress	A2A288.
Bgee	A2A288.
CleanEx	HS_ZC3H12D.
Genevestigator	A2A288.
Family and domain databases
InterPro	IPR021869. RNase_Zc3h12. IPR000571. Znf_CCCH. [Graphical view]
Pfam	PF11977. RNase_Zc3h12a. 1 hit. [Graphical view]
PROSITE	PS50103. ZF_C3H1. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	340152.
NextBio	97711.
SOURCE	Search...

Entry information

Entry name

ZC12D_HUMAN

Accession

Primary (citable) accession number: A2A288
Secondary accession number(s): A1L178 , B2RXF4, B7WNU7, B9ZZP9, B9ZZQ0, Q6ZRW2

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 2, 2008
Last sequence update:	September 1, 2009
Last modified:	May 1, 2013
This is version 56 of the entry and version 3 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.