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Protein lin-28 homolog A (Lin-28A) (Testis-expressed protein 17)

 LN28A_MOUSE             Reviewed;         209 AA.
Q8K3Y3; Q6NV62;
17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
01-OCT-2002, sequence version 1.
27-SEP-2017, entry version 126.
RecName: Full=Protein lin-28 homolog A;
Short=Lin-28A;
AltName: Full=Testis-expressed protein 17;
Name=Lin28a; Synonyms=Lin28, Tex17;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
AND DEVELOPMENTAL STAGE.
PubMed=12798299; DOI=10.1016/S0012-1606(03)00126-X;
Moss E.G., Tang L.;
"Conservation of the heterochronic regulator Lin-28, its developmental
expression and microRNA complementary sites.";
Dev. Biol. 258:432-442(2003).
[2]
ERRATUM.
Moss E.G., Tang L.;
Dev. Biol. 262:361-361(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Embryo;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
TISSUE SPECIFICITY.
PubMed=11279525; DOI=10.1038/86927;
Wang P.J., McCarrey J.R., Yang F., Page D.C.;
"An abundance of X-linked genes expressed in spermatogonia.";
Nat. Genet. 27:422-426(2001).
[5]
TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=14643679; DOI=10.1016/S1567-133X(03)00140-6;
Yang D.-H., Moss E.G.;
"Temporally regulated expression of Lin-28 in diverse tissues of the
developing mouse.";
Gene Expr. Patterns 3:719-726(2003).
[6]
INDUCTION.
PubMed=15003116; DOI=10.1186/gb-2004-5-3-r13;
Sempere L.F., Freemantle S., Pitha-Rowe I., Moss E.G., Dmitrovsky E.,
Ambros V.;
"Expression profiling of mammalian microRNAs uncovers a subset of
brain-expressed microRNAs with possible roles in murine and human
neuronal differentiation.";
Genome Biol. 5:R13.1-R13.11(2004).
[7]
TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=15722555; DOI=10.1074/jbc.M412247200;
Lee Y.S., Kim H.K., Chung S., Kim K.-S., Dutta A.;
"Depletion of human micro-RNA miR-125b reveals that it is critical for
the proliferation of differentiated cells but not for the down-
regulation of putative targets during differentiation.";
J. Biol. Chem. 280:16635-16641(2005).
[8]
INDUCTION.
PubMed=16227573; DOI=10.1128/MCB.25.21.9198-9208.2005;
Wu L., Belasco J.G.;
"Micro-RNA regulation of the mammalian lin-28 gene during neuronal
differentiation of embryonal carcinoma cells.";
Mol. Cell. Biol. 25:9198-9208(2005).
[9]
FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, INTERACTION WITH
EIF3S2, AND MUTAGENESIS OF GLY-42; 44-CYS--PHE-47; MET-81; ARG-85;
GLY-119; PRO-124; 138-ARG-CYS-139 AND CYS-142.
PubMed=17473174; DOI=10.1101/gad.415007;
Polesskaya A., Cuvellier S., Naguibneva I., Duquet A., Moss E.G.,
Harel-Bellan A.;
"Lin-28 binds IGF-2 mRNA and participates in skeletal myogenesis by
increasing translation efficiency.";
Genes Dev. 21:1125-1138(2007).
[10]
FUNCTION, AND RNA-BINDING.
PubMed=18604195; DOI=10.1038/ncb1759;
Rybak A., Fuchs H., Smirnova L., Brandt C., Pohl E.E., Nitsch R.,
Wulczyn F.G.;
"A feedback loop comprising lin-28 and let-7 controls pre-let-7
maturation during neural stem-cell commitment.";
Nat. Cell Biol. 10:987-993(2008).
[11]
FUNCTION, AND RNA-BINDING.
PubMed=18566191; DOI=10.1261/rna.1155108;
Newman M.A., Thomson J.M., Hammond S.M.;
"Lin-28 interaction with the Let-7 precursor loop mediates regulated
microRNA processing.";
RNA 14:1539-1549(2008).
[12]
FUNCTION, AND RNA-BINDING.
PubMed=18292307; DOI=10.1126/science.1154040;
Viswanathan S.R., Daley G.Q., Gregory R.I.;
"Selective blockade of microRNA processing by Lin28.";
Science 320:97-100(2008).
[13]
FUNCTION IN MAINTENANCE OF EMBRYONIC STEM CELL PLURIPOTENCY.
PubMed=19703396; DOI=10.1016/j.cell.2009.08.002;
Heo I., Joo C., Kim Y.-K., Ha M., Yoon M.-J., Cho J., Yeom K.-H.,
Han J., Kim V.N.;
"TUT4 in concert with Lin28 suppresses MicroRNA biogenesis through
pre-microRNA uridylation.";
Cell 138:696-708(2009).
[14]
FUNCTION, RNA-BINDING, AND SUBCELLULAR LOCATION.
PubMed=23102813; DOI=10.1016/j.cell.2012.10.019;
Cho J., Chang H., Kwon S.C., Kim B., Kim Y., Choe J., Ha M., Kim Y.K.,
Kim V.N.;
"LIN28A is a suppressor of ER-associated translation in embryonic stem
cells.";
Cell 151:765-777(2012).
[15]
FUNCTION.
PubMed=24209617; DOI=10.1016/j.cell.2013.09.059;
Shyh-Chang N., Zhu H., Yvanka de Soysa T., Shinoda G., Seligson M.T.,
Tsanov K.M., Nguyen L., Asara J.M., Cantley L.C., Daley G.Q.;
"Lin28 enhances tissue repair by reprogramming cellular metabolism.";
Cell 155:778-792(2013).
[16]
FUNCTION.
PubMed=26045559; DOI=10.1074/jbc.M115.665521;
O'Day E., Le M.T., Imai S., Tan S.M., Kirchner R., Arthanari H.,
Hofmann O., Wagner G., Lieberman J.;
"An RNA-binding Protein, Lin28, Recognizes and Remodels G-quartets in
the MicroRNAs (miRNAs) and mRNAs It Regulates.";
J. Biol. Chem. 290:17909-17922(2015).
[17]
X-RAY CRYSTALLOGRAPHY (2.01 ANGSTROMS) OF 31-187 IN COMPLEX WITH LET-7
RNA PRECURSORS, DOMAINS, AND SUBUNIT.
PubMed=22078496; DOI=10.1016/j.cell.2011.10.020;
Nam Y., Chen C., Gregory R.I., Chou J.J., Sliz P.;
"Molecular basis for interaction of let-7 microRNAs with Lin28.";
Cell 147:1080-1091(2011).
-!- FUNCTION: RNA-binding protein that inhibits processing of pre-let-
7 miRNAs and regulates translation of mRNAs that control
developmental timing, pluripotency and metabolism
(PubMed:17473174, PubMed:18604195, PubMed:18566191,
PubMed:18292307, PubMed:19703396, PubMed:23102813,
PubMed:24209617). Seems to recognize a common structural G-quartet
(G4) feature in its miRNA and mRNA targets (PubMed:26045559).
'Translational enhancer' that drives specific mRNAs to polysomes
and increases the efficiency of protein synthesis. Its association
with the translational machinery and target mRNAs results in an
increased number of initiation events per molecule of mRNA and,
indirectly, in mRNA stabilization. Binds IGF2 mRNA, MYOD1 mRNA,
ARBP/36B4 ribosomal protein mRNA and its own mRNA. Essential for
skeletal muscle differentiation program through the translational
up-regulation of IGF2 expression (PubMed:17473174). Suppressor of
microRNA (miRNA) biogenesis, including that of let-7, miR107, miR-
143 and miR-200c. Specifically binds the miRNA precursors (pre-
miRNAs), recognizing an 5'-GGAG-3' motif found in pre-miRNA
terminal loop, and recruits ZCCHC11/TUT4 uridylyltransferase. This
results in the terminal uridylation of target pre-miRNAs.
Uridylated pre-miRNAs fail to be processed by Dicer and undergo
degradation. The repression of let-7 expression is required for
normal development and contributes to maintain the pluripotent
state by preventing let-7-mediated differentiation of embryonic
stem cells (PubMed:19703396). Localized to the periendoplasmic
reticulum area, binds to a large number of spliced mRNAs and
inhibits the translation of mRNAs destined for the ER, reducing
the synthesis of transmembrane proteins, ER or Golgi lumen
proteins, and secretory proteins (PubMed:23102813). Binds to and
enhances the translation of mRNAs for several metabolic enzymes,
such as PFKP, PDHA1 or SDHA, increasing glycolysis and oxidative
phosphorylation. Which, with the let-7 repression may enhance
tissue repair in adult tissue (PubMed:24209617).
{ECO:0000269|PubMed:17473174, ECO:0000269|PubMed:18292307,
ECO:0000269|PubMed:18566191, ECO:0000269|PubMed:18604195,
ECO:0000269|PubMed:19703396, ECO:0000269|PubMed:23102813,
ECO:0000269|PubMed:24209617, ECO:0000269|PubMed:26045559}.
-!- SUBUNIT: Monomer (PubMed:22078496). During skeletal muscle
differentiation, associated with translation initiation complexes
in the polysomal compartment (By similarity). Directly interacts
with EIF3S2 (PubMed:17473174). Interacts with NCL in an RNA-
dependent manner. Interacts with ZCCHC11/TUT4 in the presence of
pre-let-7 RNA (By similarity). {ECO:0000250,
ECO:0000250|UniProtKB:Q9H9Z2, ECO:0000269|PubMed:17473174,
ECO:0000269|PubMed:22078496}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9H9Z2}.
Rough endoplasmic reticulum {ECO:0000269|PubMed:23102813}.
Nucleus, nucleolus. Note=Predominantly cytoplasmic. Shuttles
between the cytoplasm and the nucleus. Localizes to cytoplasmic
processing bodies and stress granules (By similarity). Nucleolar
localization observed in 10-15% of the nuclei in differentiated
myotubes. {ECO:0000250, ECO:0000250|UniProtKB:Q9H9Z2}.
-!- TISSUE SPECIFICITY: Expressed in embryonic stem cells (ES cells),
spermatagonia and testis. Expressed in numerous epithelial tissues
including the epithelia of the small intestine, the intralobular
duct epithelium of the mammary gland and the epithelia of Henle's
loop in the kidney and in the collecting duct (at protein level).
Also expressed in the myocardium and skeletal muscle (at protein
level). {ECO:0000269|PubMed:11279525, ECO:0000269|PubMed:12798299,
ECO:0000269|PubMed:14643679, ECO:0000269|PubMed:15722555}.
-!- DEVELOPMENTAL STAGE: Strongly expressed throughout the whole
embryo at 6.5 dpc, including the embryonic and extraembryonic
ectoderm and endoderm (at protein level). Subsequently expressed
in the ectoderm, endoderm and mesoderm at 7.5 dpc (at protein
level). At 9.5 dpc, expressed in epithelia covering the first
branchial arch and the coelomic cavity, the myocardium of the
developing heart, the neuroepithelium and some extraembryonic
tissues such as the visceral yolk sac (at protein level).
Expression persists in a variety of epithelial tissues at 10.5
dpc. At 15.5 dpc, expression is lost in bronchial epithelium and
becomes weaker in neuroepithelium, while increasing in the myotome
of somites, the foregut epithelium, stratified epithelium and some
kidney tubules (at protein level). At 17.5 dpc, expression
persists in the myocardium and in the epithelium covering the body
surface and skeletal muscles (at protein level). Expression is
reduced during differentiation of ES cells. In adult primary
myoblasts, barely detectable during proliferation, but
dramatically up-regulated during terminal differentiation. Induced
as early as 24 hours after differentiation signal and remains high
as late as 7 days of differentiation. Little expression in resting
muscle, but strongly up-regulated during regeneration of skeletal
muscle fibers. Expression decreases when regeneration is
histologically and functionally complete.
{ECO:0000269|PubMed:12798299, ECO:0000269|PubMed:14643679,
ECO:0000269|PubMed:15722555, ECO:0000269|PubMed:17473174}.
-!- INDUCTION: Negatively regulated by the microRNA miR-125b in
response to retinoic acid. {ECO:0000269|PubMed:15003116,
ECO:0000269|PubMed:16227573}.
-!- DOMAIN: The CSD domain is required for function in muscle
differentiation. {ECO:0000269|PubMed:22078496}.
-!- DOMAIN: The CCHC zinc fingers interact with the GGAG motif at the
3' end of let-7 miRNAs precursors, more generally they bind the
5'-NGNNG-3' consensus motif with micromolar affinity. The CSD
domain recognizes the loop at the 5' end. The flexible linker
allows accommodating variable sequences and lengths among let-7
family members. {ECO:0000269|PubMed:22078496}.
-!- MISCELLANEOUS: Reactivation of LIN28A expression enhances tissue
repair in some adult tissues by reprogramming cellular
bioenergetics. Improves hair regrowth by promoting anagen in hair
follicle and accelerates regrowth of cartilage, bone and
mesenchyme after ear and digit injuries.
{ECO:0000269|PubMed:24209617}.
-!- SIMILARITY: Belongs to the lin-28 family. {ECO:0000305}.
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EMBL; AF521097; AAM77749.1; -; mRNA.
EMBL; BC068304; AAH68304.1; -; mRNA.
CCDS; CCDS18761.1; -.
RefSeq; NP_665832.1; NM_145833.1.
UniGene; Mm.302567; -.
PDB; 3TRZ; X-ray; 2.90 A; A/B/C/D/E/F=31-187.
PDB; 3TS0; X-ray; 2.76 A; A/B=33-187.
PDB; 3TS2; X-ray; 2.01 A; A/B=31-187.
PDBsum; 3TRZ; -.
PDBsum; 3TS0; -.
PDBsum; 3TS2; -.
ProteinModelPortal; Q8K3Y3; -.
SMR; Q8K3Y3; -.
BioGrid; 219943; 7.
DIP; DIP-48573N; -.
IntAct; Q8K3Y3; 3.
STRING; 10090.ENSMUSP00000050488; -.
iPTMnet; Q8K3Y3; -.
PhosphoSitePlus; Q8K3Y3; -.
MaxQB; Q8K3Y3; -.
PaxDb; Q8K3Y3; -.
PeptideAtlas; Q8K3Y3; -.
PRIDE; Q8K3Y3; -.
Ensembl; ENSMUST00000051674; ENSMUSP00000050488; ENSMUSG00000050966.
GeneID; 83557; -.
KEGG; mmu:83557; -.
UCSC; uc008vdw.1; mouse.
CTD; 79727; -.
MGI; MGI:1890546; Lin28a.
eggNOG; KOG3070; Eukaryota.
eggNOG; COG1278; LUCA.
GeneTree; ENSGT00880000137959; -.
HOGENOM; HOG000047091; -.
HOVERGEN; HBG081922; -.
InParanoid; Q8K3Y3; -.
KO; K18754; -.
OMA; SGICKWF; -.
OrthoDB; EOG091G0RTY; -.
PhylomeDB; Q8K3Y3; -.
TreeFam; TF316240; -.
PRO; PR:Q8K3Y3; -.
Proteomes; UP000000589; Chromosome 4.
Bgee; ENSMUSG00000050966; -.
CleanEx; MM_LIN28; -.
ExpressionAtlas; Q8K3Y3; baseline and differential.
Genevisible; Q8K3Y3; MM.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0010494; C:cytoplasmic stress granule; ISS:UniProtKB.
GO; GO:0030529; C:intracellular ribonucleoprotein complex; ISS:UniProtKB.
GO; GO:0005730; C:nucleolus; IDA:MGI.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0000932; C:P-body; ISS:UniProtKB.
GO; GO:0005844; C:polysome; ISS:UniProtKB.
GO; GO:0005791; C:rough endoplasmic reticulum; IDA:UniProtKB.
GO; GO:0003677; F:DNA binding; IEA:InterPro.
GO; GO:0002151; F:G-quadruplex RNA binding; IDA:UniProtKB.
GO; GO:0035198; F:miRNA binding; IDA:UniProtKB.
GO; GO:0003729; F:mRNA binding; IDA:MGI.
GO; GO:1905538; F:polysome binding; ISS:UniProtKB.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:1990825; F:sequence-specific mRNA binding; IDA:UniProtKB.
GO; GO:0031369; F:translation initiation factor binding; IPI:MGI.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0071333; P:cellular response to glucose stimulus; IMP:BHF-UCL.
GO; GO:0007281; P:germ cell development; IMP:MGI.
GO; GO:0010587; P:miRNA catabolic process; IMP:UniProtKB.
GO; GO:0010586; P:miRNA metabolic process; IDA:MGI.
GO; GO:0045686; P:negative regulation of glial cell differentiation; IDA:MGI.
GO; GO:0017148; P:negative regulation of translation; IDA:UniProtKB.
GO; GO:1901724; P:positive regulation of cell proliferation involved in kidney development; IMP:BHF-UCL.
GO; GO:2000767; P:positive regulation of cytoplasmic translation; ISS:UniProtKB.
GO; GO:0045666; P:positive regulation of neuron differentiation; IDA:MGI.
GO; GO:1903800; P:positive regulation of production of miRNAs involved in gene silencing by miRNA; IDA:BHF-UCL.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; IDA:BHF-UCL.
GO; GO:0032008; P:positive regulation of TOR signaling; IDA:BHF-UCL.
GO; GO:0045727; P:positive regulation of translation; IDA:MGI.
GO; GO:0031054; P:pre-miRNA processing; IDA:MGI.
GO; GO:0060964; P:regulation of gene silencing by miRNA; IGI:MGI.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
GO; GO:0031123; P:RNA 3'-end processing; ISO:MGI.
GO; GO:0048863; P:stem cell differentiation; IMP:UniProtKB.
GO; GO:0019827; P:stem cell population maintenance; ISO:MGI.
CDD; cd04458; CSP_CDS; 1.
Gene3D; 4.10.60.10; -; 2.
InterPro; IPR011129; CSD.
InterPro; IPR002059; CSP_DNA-bd.
InterPro; IPR012340; NA-bd_OB-fold.
InterPro; IPR001878; Znf_CCHC.
Pfam; PF00313; CSD; 1.
Pfam; PF00098; zf-CCHC; 1.
PRINTS; PR00050; COLDSHOCK.
SMART; SM00357; CSP; 1.
SMART; SM00343; ZnF_C2HC; 2.
SUPFAM; SSF50249; SSF50249; 1.
SUPFAM; SSF57756; SSF57756; 1.
PROSITE; PS50158; ZF_CCHC; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome; Cytoplasm;
Endoplasmic reticulum; Metal-binding; Nucleus; Phosphoprotein;
Reference proteome; Repeat; RNA-binding; RNA-mediated gene silencing;
Zinc; Zinc-finger.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:Q9H9Z2}.
CHAIN 2 209 Protein lin-28 homolog A.
/FTId=PRO_0000253788.
DOMAIN 39 112 CSD.
ZN_FING 137 154 CCHC-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00047}.
ZN_FING 159 176 CCHC-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00047}.
REGION 113 136 Flexible linker.
MOD_RES 2 2 N-acetylglycine.
{ECO:0000250|UniProtKB:Q9H9Z2}.
MOD_RES 3 3 Phosphoserine.
{ECO:0000250|UniProtKB:Q9H9Z2}.
MOD_RES 120 120 Phosphoserine.
{ECO:0000250|UniProtKB:Q9H9Z2}.
MOD_RES 200 200 Phosphoserine.
{ECO:0000250|UniProtKB:Q9H9Z2}.
MUTAGEN 42 42 G->S: Erroneous subcellular location. No
positive effect on terminal myogenic
differentiation.
{ECO:0000269|PubMed:17473174}.
MUTAGEN 44 47 Missing: Erroneous subcellular location.
No positive effect on terminal myogenic
differentiation.
{ECO:0000269|PubMed:17473174}.
MUTAGEN 81 81 M->I: Erroneous subcellular location;
when associated with Q-85. No positive
effect on terminal myogenic
differentiation; when associated with Q-
85. {ECO:0000269|PubMed:17473174}.
MUTAGEN 85 85 R->Q: Erroneous subcellular location;
when associated with I-81. No positive
effect on terminal myogenic
differentiation; when associated with I-
81. {ECO:0000269|PubMed:17473174}.
MUTAGEN 119 119 G->R: Erroneous subcellular location;
when associated with S-124. No positive
effect on terminal myogenic
differentiation; when associated with S-
124. {ECO:0000269|PubMed:17473174}.
MUTAGEN 124 124 P->S: Erroneous subcellular location;
when associated with R-119. No positive
effect on terminal myogenic
differentiation; when associated with R-
119. {ECO:0000269|PubMed:17473174}.
MUTAGEN 138 139 Missing: No effect on subcellular
location; when associated with S-142.
Normal terminal myogenic differentiation;
when associated with S-142.
{ECO:0000269|PubMed:17473174}.
MUTAGEN 142 142 C->S: No effect on subcellular location;
when associated with 44-C--F-47. Normal
terminal myogenic differentiation; when
associated with 44-C--F-47.
{ECO:0000269|PubMed:17473174}.
CONFLICT 194 194 E -> D (in Ref. 3; AAH68304).
{ECO:0000305}.
STRAND 38 48 {ECO:0000244|PDB:3TS2}.
TURN 49 52 {ECO:0000244|PDB:3TS2}.
STRAND 53 61 {ECO:0000244|PDB:3TS2}.
STRAND 64 75 {ECO:0000244|PDB:3TS2}.
HELIX 76 78 {ECO:0000244|PDB:3TS2}.
STRAND 81 84 {ECO:0000244|PDB:3TS2}.
STRAND 92 100 {ECO:0000244|PDB:3TS2}.
STRAND 103 111 {ECO:0000244|PDB:3TS2}.
HELIX 112 114 {ECO:0000244|PDB:3TS2}.
TURN 124 126 {ECO:0000244|PDB:3TS0}.
TURN 140 142 {ECO:0000244|PDB:3TS2}.
HELIX 149 151 {ECO:0000244|PDB:3TS2}.
TURN 162 164 {ECO:0000244|PDB:3TS2}.
HELIX 171 173 {ECO:0000244|PDB:3TS2}.
TURN 175 178 {ECO:0000244|PDB:3TS2}.
SEQUENCE 209 AA; 22720 MW; 4BD14DCAF13CD659 CRC64;
MGSVSNQQFA GGCAKAAEKA PEEAPPDAAR AADEPQLLHG AGICKWFNVR MGFGFLSMTA
RAGVALDPPV DVFVHQSKLH MEGFRSLKEG EAVEFTFKKS AKGLESIRVT GPGGVFCIGS
ERRPKGKNMQ KRRSKGDRCY NCGGLDHHAK ECKLPPQPKK CHFCQSINHM VASCPLKAQQ
GPSSQGKPAY FREEEEEIHS PALLPEAQN


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EIAAB42013 Chicken,Gallus gallus,RCJMB04_3d16,Testis-expressed sequence 10 protein homolog,TEX10
25-844 TRIM49 contains a RING zinc finger, a motif known to be involved in protein-protein interactions. This protein has been found to be preferentially expressed in testis.The protein encoded by this gene 0.05 mg
EIAAB11306 DnaJ homolog subfamily B member 13,DNAJB13,Homo sapiens,Human,Testis and spermatogenesis cell-related protein 6,Testis spermatocyte apoptosis-related gene 6 protein,Testis spermatogenesis apoptosis-re
EIAAB11305 DnaJ homolog subfamily B member 13,Dnajb13,Mouse,Mus musculus,Testis and spermatogenesis cell-related protein 6,Testis spermatocyte apoptosis-related gene 6 protein,Testis spermatogenesis apoptosis-re
EIAAB44586 Mouse,Mus musculus,TES101-reactive protein,TES101RP,Testis-expressed protein 101,Tex101
EIAAB44357 CASK-interacting nucleosome assembly protein,Cinap,Dentt,Differentially-expressed nucleolar TGF-beta1 target protein,DXBwg1396e,Mouse,Mus musculus,Testis-specific Y-encoded-like protein 2,Tspx,Tspyl2,
EIAAB29948 Acrosomal vesicle protein HEL-127,Homo sapiens,Human,PATE3,PATE-DJ,PATE-like protein DJ,Prostate and testis expressed protein 3
EIAAB30842 Mouse,mPCl1,Mus musculus,PHD finger protein 1,Phf1,Plc1,Polycomb-like protein 1,Protein PHF1,T-complex testis-expressed 3,Tctex3,Tctex-3


 

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