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Protein

Zinc finger protein 36, C3H1 type-like 2

Gene

ZFP36L2

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

Functioni

mRNA-binding protein that plays a key role in self-renewal of erythroid cells in response to glucocorticoids. Specifically binds to the AU-rich element (ARE) in the 3'-UTR of target mRNAs, promoting their deadenylation and degradation (PubMed:14981510). Specifically expressed in burst-forming unit-erythroid (BFU-E) progenitors in response to glucocorticoids and acts as a negative regulator of erythroid cell differentiation: promotes self-renewal of erythroid cells by binding mRNAs that are induced or highly expressed during terminal erythroid differentiation and promotes their degradation, preventing erythroid cell differentiation. Down-regulated during erythroid differentiation from the BFU-E stage, stabilizing mRNAs required for terminal differentiation (By similarity).By similarity1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri153 – 18129C3H1-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri191 – 21929C3H1-type 2PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • AU-rich element binding Source: UniProtKB
  • DNA binding Source: UniProtKB-KW
  • metal ion binding Source: UniProtKB-KW
  • mRNA 3'-UTR AU-rich region binding Source: Ensembl
  • poly(A) RNA binding Source: UniProtKB
  • transcription factor activity, sequence-specific DNA binding Source: ProtInc

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

DNA-binding, Metal-binding, RNA-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Zinc finger protein 36, C3H1 type-like 2
Short name:
ZFP36-like 2
Alternative name(s):
Butyrate response factor 2
EGF-response factor 2
Short name:
ERF-2
Protein TIS11D
Gene namesi
Name:ZFP36L2
Synonyms:BRF2, ERF2, RNF162C, TIS11D
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:1108. ZFP36L2.

Subcellular locationi

  • Cytoplasm By similarity
  • Nucleus By similarity

  • Note: Shuttles between the nucleus and the cytoplasm.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

Defects in ZFP36L2 may be a cause of leukemias. Frameshfits mutations disrupting ZFP36L2 have been found in a patient with acute myeloid leukemia (PubMed:21109922).

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi157 – 1571E → R: Impaired mRNA-binding; when associated with K-195. 1 Publication
Mutagenesisi195 – 1951E → K: Impaired mRNA-binding; when associated with R-157. 1 Publication

Organism-specific databases

PharmGKBiPA35028.

Polymorphism and mutation databases

BioMutaiZFP36L2.
DMDMi146291085.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 494494Zinc finger protein 36, C3H1 type-like 2PRO_0000089170Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei57 – 571PhosphoserineCombined sources
Modified residuei125 – 1251PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiP47974.
MaxQBiP47974.
PaxDbiP47974.
PRIDEiP47974.

PTM databases

iPTMnetiP47974.
PhosphoSiteiP47974.

Expressioni

Gene expression databases

BgeeiP47974.
CleanExiHS_BRF2.
HS_ZFP36L2.
ExpressionAtlasiP47974. baseline and differential.
GenevisibleiP47974. HS.

Organism-specific databases

HPAiHPA047428.

Interactioni

Protein-protein interaction databases

BioGridi107145. 8 interactions.
IntActiP47974. 8 interactions.
STRINGi9606.ENSP00000282388.

Structurei

Secondary structure

1
494
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni152 – 1554Combined sources
Beta strandi156 – 1583Combined sources
Helixi160 – 1656Combined sources
Helixi171 – 1733Combined sources
Beta strandi175 – 1795Combined sources
Helixi180 – 1823Combined sources
Turni190 – 1934Combined sources
Helixi198 – 2036Combined sources
Helixi209 – 2113Combined sources
Beta strandi213 – 2153Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RGONMR-A151-220[»]
ProteinModelPortaliP47974.
SMRiP47974. Positions 151-220.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP47974.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni170 – 21142RNA-bindingAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi153 – 1586RNA-binding

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi106 – 1094Poly-Gly
Compositional biasi138 – 1414Poly-Gln
Compositional biasi143 – 1464Poly-Gly
Compositional biasi288 – 2914Poly-Pro
Compositional biasi323 – 33210Poly-Ala
Compositional biasi384 – 3907Poly-Ala
Compositional biasi395 – 4017Poly-Gln

Sequence similaritiesi

Contains 2 C3H1-type zinc fingers.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri153 – 18129C3H1-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri191 – 21929C3H1-type 2PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG1677. Eukaryota.
COG5063. LUCA.
GeneTreeiENSGT00530000063262.
HOGENOMiHOG000233479.
HOVERGENiHBG008483.
InParanoidiP47974.
KOiK18753.
OMAiQRDRPKL.
OrthoDBiEOG76QFJP.
PhylomeDBiP47974.
TreeFamiTF315463.

Family and domain databases

Gene3Di4.10.1000.10. 2 hits.
InterProiIPR007635. Tis11B_N.
IPR000571. Znf_CCCH.
[Graphical view]
PfamiPF04553. Tis11B_N. 1 hit.
PF00642. zf-CCCH. 2 hits.
[Graphical view]
SMARTiSM00356. ZnF_C3H1. 2 hits.
[Graphical view]
SUPFAMiSSF90229. SSF90229. 2 hits.
PROSITEiPS50103. ZF_C3H1. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P47974-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTTLLSAFY DVDFLCKTEK SLANLNLNNM LDKKAVGTPV AAAPSSGFAP
60 70 80 90 100
GFLRRHSASN LHALAHPAPS PGSCSPKFPG AANGSSCGSA AAGGPTSYGT
110 120 130 140 150
LKEPSGGGGT ALLNKENKFR DRSFSENGDR SQHLLHLQQQ QKGGGGSQIN
160 170 180 190 200
STRYKTELCR PFEESGTCKY GEKCQFAHGF HELRSLTRHP KYKTELCRTF
210 220 230 240 250
HTIGFCPYGP RCHFIHNADE RRPAPSGGAS GDLRAFGTRD ALHLGFPREP
260 270 280 290 300
RPKLHHSLSF SGFPSGHHQP PGGLESPLLL DSPTSRTPPP PSCSSASSCS
310 320 330 340 350
SSASSCSSAS AASTPSGAPT CCASAAAAAA AALLYGTGGA EDLLAPGAPC
360 370 380 390 400
AACSSASCAN NAFAFGPELS SLITPLAIQT HNFAAVAAAA YYRSQQQQQQ
410 420 430 440 450
QGLAPPAQPP APPSATLPAG AAAPPSPPFS FQLPRRLSDS PVFDAPPSPP
460 470 480 490
DSLSDRDSYL SGSLSSGSLS GSESPSLDPG RRLPIFSRLS ISDD
Length:494
Mass (Da):51,063
Last modified:May 1, 2007 - v3
Checksum:i10E23FA9E2DDABD4
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti96 – 972TS → DL in AAA91778 (PubMed:8545129).Curated
Sequence conflicti318 – 3181A → T in CAA55592 (PubMed:7835719).Curated
Sequence conflicti329 – 3324AAAA → LR in CAA55592 (PubMed:7835719).Curated
Sequence conflicti331 – 3322Missing in AAA91778 (PubMed:8545129).Curated
Sequence conflicti400 – 4001Q → QQQQ in AAH05010 (PubMed:15489334).Curated
Sequence conflicti453 – 46210Missing in AAA91778 (PubMed:8545129).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U07802 Genomic DNA. Translation: AAA91778.1.
X78992 mRNA. Translation: CAA55592.1.
AC010883 Genomic DNA. Translation: AAY14992.1.
CH471053 Genomic DNA. Translation: EAX00306.1.
BC005010 mRNA. Translation: AAH05010.1.
CCDSiCCDS1811.1.
PIRiS49147.
RefSeqiNP_008818.3. NM_006887.4.
UniGeneiHs.503093.

Genome annotation databases

EnsembliENST00000282388; ENSP00000282388; ENSG00000152518.
GeneIDi678.
KEGGihsa:678.
UCSCiuc002rsv.5. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U07802 Genomic DNA. Translation: AAA91778.1.
X78992 mRNA. Translation: CAA55592.1.
AC010883 Genomic DNA. Translation: AAY14992.1.
CH471053 Genomic DNA. Translation: EAX00306.1.
BC005010 mRNA. Translation: AAH05010.1.
CCDSiCCDS1811.1.
PIRiS49147.
RefSeqiNP_008818.3. NM_006887.4.
UniGeneiHs.503093.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RGONMR-A151-220[»]
ProteinModelPortaliP47974.
SMRiP47974. Positions 151-220.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107145. 8 interactions.
IntActiP47974. 8 interactions.
STRINGi9606.ENSP00000282388.

PTM databases

iPTMnetiP47974.
PhosphoSiteiP47974.

Polymorphism and mutation databases

BioMutaiZFP36L2.
DMDMi146291085.

Proteomic databases

EPDiP47974.
MaxQBiP47974.
PaxDbiP47974.
PRIDEiP47974.

Protocols and materials databases

DNASUi678.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000282388; ENSP00000282388; ENSG00000152518.
GeneIDi678.
KEGGihsa:678.
UCSCiuc002rsv.5. human.

Organism-specific databases

CTDi678.
GeneCardsiZFP36L2.
HGNCiHGNC:1108. ZFP36L2.
HPAiHPA047428.
MIMi612053. gene.
neXtProtiNX_P47974.
PharmGKBiPA35028.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1677. Eukaryota.
COG5063. LUCA.
GeneTreeiENSGT00530000063262.
HOGENOMiHOG000233479.
HOVERGENiHBG008483.
InParanoidiP47974.
KOiK18753.
OMAiQRDRPKL.
OrthoDBiEOG76QFJP.
PhylomeDBiP47974.
TreeFamiTF315463.

Miscellaneous databases

ChiTaRSiZFP36L2. human.
EvolutionaryTraceiP47974.
GenomeRNAii678.
PROiP47974.
SOURCEiSearch...

Gene expression databases

BgeeiP47974.
CleanExiHS_BRF2.
HS_ZFP36L2.
ExpressionAtlasiP47974. baseline and differential.
GenevisibleiP47974. HS.

Family and domain databases

Gene3Di4.10.1000.10. 2 hits.
InterProiIPR007635. Tis11B_N.
IPR000571. Znf_CCCH.
[Graphical view]
PfamiPF04553. Tis11B_N. 1 hit.
PF00642. zf-CCCH. 2 hits.
[Graphical view]
SMARTiSM00356. ZnF_C3H1. 2 hits.
[Graphical view]
SUPFAMiSSF90229. SSF90229. 2 hits.
PROSITEiPS50103. ZF_C3H1. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of a member of the TIS11 early response gene family at the insertion point of a DNA fragment containing a gene for the T-cell receptor beta chain in an acute T-cell leukemia."
    Ino T., Yasui H., Hirano M., Kurosawa Y.
    Oncogene 11:2705-2710(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "ERF-2, the human homologue of the murine Tis11d early response gene."
    Nie X.F., Maclean K.N., Kumar V., McKay I.A., Bustin S.A.
    Gene 152:285-286(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. 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: Pancreas.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "A computational study of RNA binding and specificity in the tandem zinc finger domain of TIS11d."
    Morgan B.R., Massi F.
    Protein Sci. 19:1222-1234(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: RNA-BINDING, MUTAGENESIS OF GLU-157 AND GLU-195.
  8. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "Mutation in the RNA binding protein TIS11D/ZFP36L2 is associated with the pathogenesis of acute leukemia."
    Iwanaga E., Nanri T., Mitsuya H., Asou N.
    Int. J. Oncol. 38:25-31(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: POSSIBLE INVOLVEMENT IN LEUKEMIAS.
  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-125, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  12. "Recognition of the mRNA AU-rich element by the zinc finger domain of TIS11d."
    Hudson B.P., Martinez-Yamout M.A., Dyson H.J., Wright P.E.
    Nat. Struct. Mol. Biol. 11:257-264(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 151-220 IN COMPLEX WITH RNA, FUNCTION, RNA-BINDING.

Entry informationi

Entry nameiTISD_HUMAN
AccessioniPrimary (citable) accession number: P47974
Secondary accession number(s): Q53TB4, Q9BSJ3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: May 1, 2007
Last modified: June 8, 2016
This is version 152 of the entry and version 3 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.