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Ectoderm-neural cortex protein 1 (ENC-1) (Kelch-like protein 37) (Nuclear matrix protein NRP/B) (p53-induced gene 10 protein)

 ENC1_HUMAN              Reviewed;         589 AA.
O14682; B4DHJ1; E9PFU0; O75464; Q9UPG9;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
01-DEC-2000, sequence version 2.
12-SEP-2018, entry version 169.
RecName: Full=Ectoderm-neural cortex protein 1;
Short=ENC-1;
AltName: Full=Kelch-like protein 37;
AltName: Full=Nuclear matrix protein NRP/B;
AltName: Full=p53-induced gene 10 protein;
Name=ENC1; Synonyms=KLHL37, NRPB, PIG10;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INDUCTION BY TP53.
TISSUE=Colon cancer;
PubMed=9305847; DOI=10.1038/38525;
Polyak K., Xia Y., Zweier J.L., Kinzler K.W., Vogelstein B.;
"A model for p53-induced apoptosis.";
Nature 389:300-306(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=9683534; DOI=10.1006/excr.1998.4109;
Hernandez M.-C., Andres-Barquin P.J., Holt I., Israel M.A.;
"Cloning of human ENC-1 and evaluation of its expression and
regulation in nervous system tumors.";
Exp. Cell Res. 242:470-477(1998).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Fetal brain, and Hippocampus;
PubMed=9566959; DOI=10.1083/jcb.141.3.553;
Kim T.-A., Lim J., Ota S., Raja S., Rogers R., Rivnay B., Avraham H.,
Avraham S.;
"NRP/B, a novel nuclear matrix protein, associates with p110(RB) and
is involved in neuronal differentiation.";
J. Cell Biol. 141:553-566(1998).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Brain;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15372022; DOI=10.1038/nature02919;
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T.,
Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M.,
Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K.,
Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C.,
Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M.,
Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A.,
Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M.,
Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M.,
Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S.,
Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
"The DNA sequence and comparative analysis of human chromosome 5.";
Nature 431:268-274(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Muscle;
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).
[7]
IDENTIFICATION IN A COMPLEX WITH CUL3 AND RBX1, AND UBIQUITINATION.
PubMed=15983046; DOI=10.1074/jbc.M501279200;
Zhang D.D., Lo S.C., Sun Z., Habib G.M., Lieberman M.W., Hannink M.;
"Ubiquitination of Keap1, a BTB-Kelch substrate adaptor protein for
Cul3, targets Keap1 for degradation by a proteasome-independent
pathway.";
J. Biol. Chem. 280:30091-30099(2005).
[8]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH KEAP1.
PubMed=19424503; DOI=10.1371/journal.pone.0005492;
Wang X.J., Zhang D.D.;
"Ectodermal-neural cortex 1 down-regulates Nrf2 at the translational
level.";
PLoS ONE 4:E5492-E5492(2009).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
-!- FUNCTION: Actin-binding protein involved in the regulation of
neuronal process formation and in differentiation of neural crest
cells. Down-regulates transcription factor NF2L2/NRF2 by
decreasing the rate of protein synthesis and not via a ubiquitin-
mediated proteasomal degradation mechanism.
{ECO:0000269|PubMed:19424503}.
-!- SUBUNIT: Binds to RB1. Hypophosphorylated RB1 associates with ENC1
during neuronal differentiation, while hyperphosphorylated RB1
associates with ENC1 in undifferentiating cells. Part of a complex
that contains CUL3, RBX1 and ENC1. Interacts indirectly with
KEAP1. {ECO:0000269|PubMed:15983046, ECO:0000269|PubMed:19424503}.
-!- SUBCELLULAR LOCATION: Nucleus matrix
{ECO:0000269|PubMed:19424503}. Cytoplasm
{ECO:0000269|PubMed:19424503}. Cytoplasm, cytoskeleton
{ECO:0000269|PubMed:19424503}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=O14682-1; Sequence=Displayed;
Name=2;
IsoId=O14682-2; Sequence=VSP_045074;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Detected in fetal brain tissue, moderate
expression in fetal heart, lung and kidney. Highly expressed in
adult brain, particularly high in the hippocampus and amygdala,
and spinal chord. Detectable in adult pancreas. May be down-
regulated in neuroblastoma tumors.
-!- DEVELOPMENTAL STAGE: Dramatically up-regulated upon neuronal
differentiation.
-!- INDUCTION: By p53/TP53. {ECO:0000269|PubMed:9305847}.
-!- PTM: Ubiquitinated by E3 ubiquitin ligase complex formed by CUL3
and RBX1 and probably targeted for proteasome-independent
degradation. Quinone-induced oxidative stress increases its
ubiquitination. {ECO:0000269|PubMed:15983046}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/NRPBID40451ch5q12.html";
-----------------------------------------------------------------------
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EMBL; AF010314; AAC39532.1; -; mRNA.
EMBL; AF005381; AAC64498.1; -; mRNA.
EMBL; AF059611; AAC26109.1; -; mRNA.
EMBL; AK295128; BAG58153.1; -; mRNA.
EMBL; AC026405; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC000418; AAH00418.1; -; mRNA.
CCDS; CCDS4021.1; -. [O14682-1]
CCDS; CCDS58958.1; -. [O14682-2]
RefSeq; NP_001243503.1; NM_001256574.1. [O14682-1]
RefSeq; NP_001243504.1; NM_001256575.1. [O14682-1]
RefSeq; NP_001243505.1; NM_001256576.1. [O14682-2]
RefSeq; NP_003624.1; NM_003633.3. [O14682-1]
RefSeq; XP_011541998.1; XM_011543696.2. [O14682-1]
RefSeq; XP_011541999.1; XM_011543697.2. [O14682-1]
UniGene; Hs.104925; -.
UniGene; Hs.744844; -.
ProteinModelPortal; O14682; -.
SMR; O14682; -.
BioGrid; 114079; 15.
IntAct; O14682; 1.
STRING; 9606.ENSP00000306356; -.
iPTMnet; O14682; -.
PhosphoSitePlus; O14682; -.
BioMuta; ENC1; -.
EPD; O14682; -.
PaxDb; O14682; -.
PeptideAtlas; O14682; -.
PRIDE; O14682; -.
ProteomicsDB; 48165; -.
DNASU; 8507; -.
Ensembl; ENST00000302351; ENSP00000306356; ENSG00000171617. [O14682-1]
Ensembl; ENST00000510316; ENSP00000423804; ENSG00000171617. [O14682-2]
Ensembl; ENST00000537006; ENSP00000446289; ENSG00000171617. [O14682-1]
Ensembl; ENST00000618628; ENSP00000479101; ENSG00000171617. [O14682-1]
GeneID; 8507; -.
KEGG; hsa:8507; -.
UCSC; uc011css.4; human. [O14682-1]
CTD; 8507; -.
DisGeNET; 8507; -.
EuPathDB; HostDB:ENSG00000171617.13; -.
GeneCards; ENC1; -.
HGNC; HGNC:3345; ENC1.
HPA; HPA078061; -.
MIM; 605173; gene.
neXtProt; NX_O14682; -.
OpenTargets; ENSG00000171617; -.
PharmGKB; PA27782; -.
eggNOG; KOG4441; Eukaryota.
eggNOG; ENOG410XNX8; LUCA.
GeneTree; ENSGT00910000143979; -.
HOGENOM; HOG000232171; -.
HOVERGEN; HBG000905; -.
InParanoid; O14682; -.
KO; K10462; -.
OMA; MNIYLFH; -.
OrthoDB; EOG091G03JU; -.
PhylomeDB; O14682; -.
TreeFam; TF329218; -.
ChiTaRS; ENC1; human.
GeneWiki; ENC1; -.
GenomeRNAi; 8507; -.
PRO; PR:O14682; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000171617; Expressed in 230 organ(s), highest expression level in Brodmann (1909) area 10.
CleanEx; HS_ENC1; -.
ExpressionAtlas; O14682; baseline and differential.
Genevisible; O14682; HS.
GO; GO:0031463; C:Cul3-RING ubiquitin ligase complex; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
GO; GO:0000790; C:nuclear chromatin; IEA:Ensembl.
GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
GO; GO:0005730; C:nucleolus; IEA:Ensembl.
GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
GO; GO:0005634; C:nucleus; TAS:ProtInc.
GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
GO; GO:0007275; P:multicellular organism development; TAS:ProtInc.
GO; GO:0017148; P:negative regulation of translation; IDA:UniProtKB.
GO; GO:0007399; P:nervous system development; TAS:ProtInc.
GO; GO:0010976; P:positive regulation of neuron projection development; IEA:Ensembl.
GO; GO:0010499; P:proteasomal ubiquitin-independent protein catabolic process; IDA:UniProtKB.
GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
Gene3D; 2.120.10.80; -; 1.
InterPro; IPR011705; BACK.
InterPro; IPR017096; BTB-kelch_protein.
InterPro; IPR000210; BTB/POZ_dom.
InterPro; IPR030562; ENC1.
InterPro; IPR015915; Kelch-typ_b-propeller.
InterPro; IPR006652; Kelch_1.
InterPro; IPR011333; SKP1/BTB/POZ_sf.
PANTHER; PTHR24410:SF5; PTHR24410:SF5; 1.
Pfam; PF07707; BACK; 1.
Pfam; PF00651; BTB; 1.
Pfam; PF01344; Kelch_1; 4.
PIRSF; PIRSF037037; Kelch-like_protein_gigaxonin; 1.
SMART; SM00875; BACK; 1.
SMART; SM00225; BTB; 1.
SMART; SM00612; Kelch; 6.
SUPFAM; SSF117281; SSF117281; 1.
SUPFAM; SSF54695; SSF54695; 1.
PROSITE; PS50097; BTB; 1.
1: Evidence at protein level;
Actin-binding; Alternative splicing; Complete proteome; Cytoplasm;
Cytoskeleton; Developmental protein; Kelch repeat; Nucleus;
Polymorphism; Reference proteome; Repeat; Ubl conjugation.
CHAIN 1 589 Ectoderm-neural cortex protein 1.
/FTId=PRO_0000119068.
DOMAIN 46 114 BTB. {ECO:0000255|PROSITE-
ProRule:PRU00037}.
REPEAT 296 340 Kelch 1.
REPEAT 341 388 Kelch 2.
REPEAT 389 444 Kelch 3.
REPEAT 446 492 Kelch 4.
REPEAT 494 538 Kelch 5.
REPEAT 539 585 Kelch 6.
VAR_SEQ 1 73 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_045074.
VARIANT 256 256 I -> S (in dbSNP:rs16872126).
/FTId=VAR_050040.
CONFLICT 108 108 S -> F (in Ref. 4; BAG58153).
{ECO:0000305}.
CONFLICT 112 130 INEENAESLLEAGDMLEFQ -> HQLEGKCRNSLLGSLVTC
WSFK (in Ref. 1). {ECO:0000305}.
CONFLICT 237 238 RL -> TR (in Ref. 1; AAC39532).
{ECO:0000305}.
CONFLICT 378 378 R -> M (in Ref. 4; BAG58153).
{ECO:0000305}.
CONFLICT 402 402 C -> S (in Ref. 2; AAC64498).
{ECO:0000305}.
CONFLICT 427 427 V -> A (in Ref. 1). {ECO:0000305}.
CONFLICT 430 438 LREGVSNAA -> RPRRRYNCAQ (in Ref. 1).
{ECO:0000305}.
CONFLICT 484 589 YTAAAVLGNQIFIMGGDTEFSACSAYKFNSETYQWTKVGDV
TAKRMSCHAVASGNKLYVVGGYFGIQRCKTLDCYDPTLDVW
NSITTVPYSLIPTAFVSTWKHLPS -> IHSQASCPGGTQD
FLLWGVIQNFSACFCL (in Ref. 1; AAC39532).
{ECO:0000305}.
SEQUENCE 589 AA; 66130 MW; DB003A1DFA65BAA0 CRC64;
MSVSVHENRK SRASSGSINI YLFHKSSYAD SVLTHLNLLR QQRLFTDVLL HAGNRTFPCH
RAVLAACSRY FEAMFSGGLK ESQDSEVNFD NSIHPEVLEL LLDYAYSSRV IINEENAESL
LEAGDMLEFQ DIRDACAEFL EKNLHPTNCL GMLLLSDAHQ CTKLYELSWR MCLSNFQTIR
KNEDFLQLPQ DMVVQLLSSE ELETEDERLV YESAINWISY DLKKRYCYLP ELLQTVRLAL
LPAIYLMENV AMEELITKQR KSKEIVEEAI RCKLKILQND GVVTSLCARP RKTGHALFLL
GGQTFMCDKL YLVDQKAKEI IPKADIPSPR KEFSACAIGC KVYITGGRGS ENGVSKDVWV
YDTLHEEWSK AAPMLVARFG HGSAELKHCL YVVGGHTAAT GCLPASPSVS LKQVEHYDPT
INKWTMVAPL REGVSNAAVV SAKLKLFAFG GTSVSHDKLP KVQCYDQCEN RWTVPATCPQ
PWRYTAAAVL GNQIFIMGGD TEFSACSAYK FNSETYQWTK VGDVTAKRMS CHAVASGNKL
YVVGGYFGIQ RCKTLDCYDP TLDVWNSITT VPYSLIPTAF VSTWKHLPS


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