O14682 (ENC1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ectoderm-neural cortex protein 1
Short name=ENC-1

Alternative name(s):
Kelch-like protein 37
Nuclear matrix protein NRP/B
p53-induced gene 10 protein

Gene names

Name:	ENC1
Synonyms:	KLHL37, NRPB, PIG10

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	589 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Actin-binding protein involved in the regulation of neuronal process formation and in differentiation of neural crest cells. May be down-regulated in neuroblastoma tumors. Substrate-specific adapter of an E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Ref.5
Pathway	Protein modification; protein ubiquitination.
Subunit structure	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.
Subcellular location	Nucleus matrix. Cytoplasm › cytoskeleton.
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.
Developmental stage	Dramatically up-regulated upon neuronal differentiation.
Induction	By p53/TP53. Ref.1
Post-translational modification	Ubiquitinated and probably targeted for proteasome-independent degradation. Ref.5
Sequence similarities	Contains 1 BTB (POZ) domain. Contains 6 Kelch repeats.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Cellular component	Cytoplasm Cytoskeleton Nucleus
Coding sequence diversity	Polymorphism
Domain	Kelch repeat Repeat
Ligand	Actin-binding
Molecular function	Developmental protein
PTM	Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	nervous system development Traceable author statement. Source: ProtInc
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW cytoskeleton Inferred from electronic annotation. Source: UniProtKB-SubCell nuclear matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	actin binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 589	589	Ectoderm-neural cortex protein 1		PRO_0000119068
Regions
	Domain	46 – 114	69	BTB
	Repeat	296 – 340	45	Kelch 1
	Repeat	341 – 388	48	Kelch 2
	Repeat	389 – 444	56	Kelch 3
	Repeat	446 – 492	47	Kelch 4
	Repeat	494 – 538	45	Kelch 5
	Repeat	539 – 585	47	Kelch 6
Amino acid modifications
	Modified residue	435	1	Phosphoserine Ref.6
	Modified residue	441	1	Phosphoserine Ref.6
Natural variations
	Natural variant	256	1	I → S. Corresponds to variant rs16872126 [ dbSNP | Ensembl ].		VAR_050040
Experimental info
	Sequence conflict	112 – 130	19	INEEN…MLEFQ → HQLEGKCRNSLLGSLVTCWS FK Ref.1
	Sequence conflict	237 – 238	2	RL → TR in AAC39532. Ref.1
	Sequence conflict	402	1	C → S in AAC64498. Ref.2
	Sequence conflict	427	1	V → A Ref.1
	Sequence conflict	430 – 438	9	LREGVSNAA → RPRRRYNCAQ Ref.1
	Sequence conflict	484 – 589	106	YTAAA…KHLPS → IHSQASCPGGTQDFLLWGVI QNFSACFCL in AAC39532. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	O14682 [UniParc]. Last modified December 1, 2000. Version 2. Checksum: DB003A1DFA65BAA0	FASTA	589	66,130
	10 20 30 40 50 60 MSVSVHENRK SRASSGSINI YLFHKSSYAD SVLTHLNLLR QQRLFTDVLL HAGNRTFPCH 70 80 90 100 110 120 RAVLAACSRY FEAMFSGGLK ESQDSEVNFD NSIHPEVLEL LLDYAYSSRV IINEENAESL 130 140 150 160 170 180 LEAGDMLEFQ DIRDACAEFL EKNLHPTNCL GMLLLSDAHQ CTKLYELSWR MCLSNFQTIR 190 200 210 220 230 240 KNEDFLQLPQ DMVVQLLSSE ELETEDERLV YESAINWISY DLKKRYCYLP ELLQTVRLAL 250 260 270 280 290 300 LPAIYLMENV AMEELITKQR KSKEIVEEAI RCKLKILQND GVVTSLCARP RKTGHALFLL 310 320 330 340 350 360 GGQTFMCDKL YLVDQKAKEI IPKADIPSPR KEFSACAIGC KVYITGGRGS ENGVSKDVWV 370 380 390 400 410 420 YDTLHEEWSK AAPMLVARFG HGSAELKHCL YVVGGHTAAT GCLPASPSVS LKQVEHYDPT 430 440 450 460 470 480 INKWTMVAPL REGVSNAAVV SAKLKLFAFG GTSVSHDKLP KVQCYDQCEN RWTVPATCPQ 490 500 510 520 530 540 PWRYTAAAVL GNQIFIMGGD TEFSACSAYK FNSETYQWTK VGDVTAKRMS CHAVASGNKL 550 560 570 580 YVVGGYFGIQ RCKTLDCYDP TLDVWNSITT VPYSLIPTAF VSTWKHLPS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A model for p53-induced apoptosis." Polyak K., Xia Y., Zweier J.L., Kinzler K.W., Vogelstein B. Nature 389:300-306(1997) [PubMed: 9305847] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION BY TP53. Tissue: Colon cancer.
[2]	"Cloning of human ENC-1 and evaluation of its expression and regulation in nervous system tumors." Hernandez M.-C., Andres-Barquin P.J., Holt I., Israel M.A. Exp. Cell Res. 242:470-477(1998) [PubMed: 9683534] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"NRP/B, a novel nuclear matrix protein, associates with p110(RB) and is involved in neuronal differentiation." Kim T.-A., Lim J., Ota S., Raja S., Rogers R., Rivnay B., Avraham H., Avraham S. J. Cell Biol. 141:553-566(1998) [PubMed: 9566959] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Fetal brain and Hippocampus.
[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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Muscle.
[5]	"Ubiquitination of Keap1, a BTB-Kelch substrate adaptor protein for Cul3, targets Keap1 for degradation by a proteasome-independent pathway." Zhang D.D., Lo S.C., Sun Z., Habib G.M., Lieberman M.W., Hannink M. J. Biol. Chem. 280:30091-30099(2005) [PubMed: 15983046] [Abstract] Cited for: FUNCTION AS A E3 UBIQUITIN-PROTEIN LIGASE, IDENTIFICATION IN A COMPLEX WITH CUL3 AND RBX1, UBIQUITINATION.
[6]	"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-435 AND SER-441, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF010314 mRNA. Translation: AAC39532.1. AF005381 mRNA. Translation: AAC64498.1. AF059611 mRNA. Translation: AAC26109.1. BC000418 mRNA. Translation: AAH00418.1.
IPI	IPI00023188.
RefSeq	NP_003624.1. NM_003633.2.
UniGene	Hs.104925.
3D structure databases
ProteinModelPortal	O14682.
SMR	O14682. Positions 18-276, 294-583.
ModBase	Search...
Protein-protein interaction databases
STRING	O14682.
PTM databases
PhosphoSite	O14682.
Proteomic databases
PRIDE	O14682.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000302351; ENSP00000306356; ENSG00000171617.
GeneID	8507.
KEGG	hsa:8507.
UCSC	uc003kdc.2. human.
Organism-specific databases
CTD	8507.
GeneCards	GC05M073958.
H-InvDB	HIX0004948.
HGNC	HGNC:3345. ENC1.
HPA	HPA030726.
MIM	605173. gene.
neXtProt	NX_O14682.
PharmGKB	PA27782.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG13815.
HOGENOM	HBG445733.
HOVERGEN	HBG000905.
InParanoid	O14682.
OMA	HCYLPEL.
OrthoDB	EOG4DJJW1.
PhylomeDB	O14682.
Gene expression databases
ArrayExpress	O14682.
Bgee	O14682.
CleanEx	HS_ENC1.
Genevestigator	O14682.
GermOnline	ENSG00000171617. Homo sapiens.
Family and domain databases
InterPro	IPR011705. BACK. IPR000210. BTB/POZ-like. IPR011333. BTB/POZ_fold. IPR013069. BTB_POZ. IPR017096. Kelch-like_gigaxonin. IPR015915. Kelch-typ_b-propeller. IPR006652. Kelch_1. [Graphical view]
Gene3D	G3DSA:3.30.710.10. BTB/POZ_fold. 1 hit. G3DSA:2.120.10.80. Kelch-typ_b-propeller. 1 hit.
KO	K10462.
Pfam	PF07707. BACK. 1 hit. PF00651. BTB. 1 hit. PF01344. Kelch_1. 4 hits. [Graphical view]
PIRSF	PIRSF037037. Kelch-like_protein_gigaxonin. 1 hit.
SMART	SM00875. BACK. 1 hit. SM00225. BTB. 1 hit. SM00612. Kelch. 6 hits. [Graphical view]
SUPFAM	SSF54695. BTB/POZ_fold. 1 hit.
PROSITE	PS50097. BTB. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	31839.
SOURCE	Search...

Entry information

Entry name

ENC1_HUMAN

Accession

Primary (citable) accession number: O14682
Secondary accession number(s): O75464, Q9UPG9

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	December 1, 2000
Last modified:	January 25, 2012
This is version 109 of the entry and version 2 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.