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FLASH GENE

Symbol

TCP1

contributors: mct/npt/pgu - updated : 27-09-2015

HGNC name	t-complex 1
HGNC id	11655

FLASH GENE DNA RNA EXPRESSION PROTEIN DISORDER ANIMAL & CELL MODELS

DNA

TYPE	functioning gene
SPECIAL FEATURE
text	overlapping in opposite sense in the 3' region of ACAT2
STRUCTURE	11.21 kb     12 Exon(s)

10 Kb 5' upstream gene genomic sequence study

MAPPING

cloned

Y

linked

Y

status

confirmed

Map

see TCP10

RNA

TRANSCRIPTS	type	messenger

identification nb exons type bp product Protein kDa AA specific expression Year Pubmed NM_030752 12 - 2463 NP_110379 - 556 - 2007 17939680 NM_001008897 11 - 2377 NP_001008897 - 401 - 2007 17939680

EXPRESSION

Type	ubiquitous

expressed in	(based on citations)
organ(s)	System Organ level 1 Organ level 2 Organ level 3 Organ level 4 Level Pubmed Species Stage Rna symbol Endocrine adrenal gland       highly Lymphoid/Immune spleen       highly   thymus       highly Reproductive male system testis     highly

cell lineage

cell lines

fluid/secretion

at STAGE

PROTEIN

PHYSICAL PROPERTIES

STRUCTURE

motifs/domains

mono polymer

heteromer

HOMOLOGY

interspecies

homolog to murine Tcp1

Homologene

FAMILY

TCP-1 chaperonin family

CATEGORY

chaperone/stress

SUBCELLULAR LOCALIZATION	plasma membrane
	intracellular
	intracellular,cytoplasm,organelle,Golgi
	intracellular,cytoplasm,cytosolic
	intracellular,cytoplasm,cytoskeleton,microtubule,centrosome
	intracellular,nucleus

basic FUNCTION	potential chaperonin
	modulating TP53-dependent function and avoid senescence
	maintains cellular protein folding homeostasis in the eukaryotic cytosol by assisting the biogenesis of many proteins, including actins, tubulins, and regulators of the cell cycle
	required for maturation of sphingosine kinase 1
	folds the cytoskeletal protein actin
	CCT complex is responsible for the folding of a number of proteins including actin and tubulin
	multi-subunit molecular machine thought to assist in the folding of 10p100 of newly translated cytosolic proteins in eukaryotes (
	normal TCP1 function is ultimately required for the morphogenesis and survival of sensory neurons of the retina, and suggest the chaperonin TCP1 deficiency as a potential, yet unexplored, cause of neurodegenerative diseases
	TCP1 complex harbor at least one putative zona pellucida binding protein, ZPBP2, playing a role in the mediation of sperm-zona pellucida interaction
	molecular chaperone TRiC/CCT is essential for correct protein folding, DYRK1A binding, and nuclear accumulation of DCAF7

CELLULAR PROCESS

protein, post translation, folding

PHYSIOLOGICAL PROCESS

PATHWAY

metabolism

signaling

a component	component of a heterooligomeric complex, 97kDa, containing
	several structurally related subunits, assembled into a TCP1 ring and mediating ATP dependent, monomeric protein folding
	part of chaperonin containing TCP1 complex (CCT), also known as the TCP1 ring complex (TRiC)
	molecular chaperones having a post-translational role in maintaining the native form of actin during its slow transport to the axon terminal and ensuring its correct assembly into microfilaments
	complex formed by two back-to-back stacked hetero-octameric rings that assists the folding of actins, tubulins, and other proteins in an ATP-dependent manner

INTERACTION

DNA

RNA

small molecule	cofactor,
	PDCL is thought to act as a TCP1 co-factor

protein	interacting with PLK1 (is required for the biogenesis of functional PLK1)
	PDCL2 physically interacts with TCP1 and modulates its folding activity
	formation of a stable complex between chaperonin-containing TCP1 and HSPA8, two eukaryotic representatives of these chaperone families
	interacts with huntingtin and results in decrease of aggregate formation followed by increase of cell survival
	TCP1 ring complex/chaperonin-containing TCP1 (TRiC/CCT) were identified as major DCAF7-binding proteins, and phosphorylation sites in both DCAF7 and TRiC/CCT were identified
	key checkpoint function for the chaperonin TCP1, which specifically associates with nascent TAF5 for subsequent handover to TAF6-TAF9 and ultimate holo-TBP formation

cell & other

REGULATION

ASSOCIATED DISORDERS

corresponding disease(s)

Other morbid association(s)

Type Gene Modification Chromosome rearrangement Protein expression Protein Function tumoral     --low   in colon carcinomas

Susceptibility

to Alzheimer disease (AD)

Variant & Polymorphism other	variant increasing risk of AD

Candidate gene

Marker

Therapy target

ANIMAL & CELL MODELS