P48643 (TCPE_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
T-complex protein 1 subunit epsilon
Short name=TCP-1-epsilon

Alternative name(s):
CCT-epsilon

Gene names

Name:	CCT5
Synonyms:	CCTE, KIAA0098

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	541 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. As part of the BBS/CCT complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. Known to play a role, in vitro, in the folding of actin and tubulin. Ref.12
Subunit structure	Heterooligomeric complex of about 850 to 900 kDa that forms two stacked rings, 12 to 16 nm in diameter. Interacts with PACRG. Component of the BBS/CCT complex composed at least of MKKS, BBS10, BBS12, TCP1, CCT2, CCT3, CCT4, CCT5 AND CCT8. Ref.8
Subcellular location	Cytoplasm. Cytoplasm › cytoskeleton › centrosome Ref.12.
Induction	Down-regulated in response to enterovirus 71 (EV71) infection (at protein level). Ref.9
Involvement in disease	Defects in CCT5 are the cause of hereditary sensory neuropathy autosomal recessive with spastic paraplegia (HSNSP) [MIM:256840]. The disease is characterized by spastic paraplegia and progressive distal sensory neuropathy leading to mutilating ulcerations of the upper and lower limbs. Ref.14
Sequence similarities	Belongs to the TCP-1 chaperonin family.
Sequence caution	The sequence BAA07894.2 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Cytoplasm Cytoskeleton
Coding sequence diversity	Polymorphism
Disease	Disease mutation Neuropathy
Ligand	ATP-binding Nucleotide-binding
Molecular function	Chaperone
PTM	Acetylation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	'de novo' posttranslational protein folding Traceable author statement. Source: Reactome response to virus Inferred from expression pattern Ref.9. Source: UniProtKB
Cellular component	microtubule organizing center Inferred from electronic annotation. Source: UniProtKB-SubCell nucleolus Inferred from direct assay. Source: HPA
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW unfolded protein binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.5 Ref.6
	Chain	2 – 541	540	T-complex protein 1 subunit epsilon		PRO_0000128346
Amino acid modifications
	Modified residue	2	1	N-acetylalanine Ref.5 Ref.6 Ref.10
	Modified residue	223	1	N6-acetyllysine Ref.11
	Modified residue	232	1	N6-acetyllysine Ref.11
	Modified residue	399	1	N6-acetyllysine Ref.11
Natural variations
	Natural variant	146	1	E → V. Corresponds to variant rs11557652 [ dbSNP | Ensembl ].		VAR_052267
	Natural variant	147	1	H → R in HSNSP. Ref.14		VAR_030658

Sequences

	Sequence		Length	Mass (Da)
	P48643 [UniParc]. Last modified February 1, 1996. Version 1. Checksum: 164168BB80EF022A	FASTA	541	59,671
	10 20 30 40 50 60 MASMGTLAFD EYGRPFLIIK DQDRKSRLMG LEALKSHIMA AKAVANTMRT SLGPNGLDKM 70 80 90 100 110 120 MVDKDGDVTV TNDGATILSM MDVDHQIAKL MVELSKSQDD EIGDGTTGVV VLAGALLEEA 130 140 150 160 170 180 EQLLDRGIHP IRIADGYEQA ARVAIEHLDK ISDSVLVDIK DTEPLIQTAK TTLGSKVVNS 190 200 210 220 230 240 CHRQMAEIAV NAVLTVADME RRDVDFELIK VEGKVGGRLE DTKLIKGVIV DKDFSHPQMP 250 260 270 280 290 300 KKVEDAKIAI LTCPFEPPKP KTKHKLDVTS VEDYKALQKY EKEKFEEMIQ QIKETGANLA 310 320 330 340 350 360 ICQWGFDDEA NHLLLQNNLP AVRWVGGPEI ELIAIATGGR IVPRFSELTA EKLGFAGLVQ 370 380 390 400 410 420 EISFGTTKDK MLVIEQCKNS RAVTIFIRGG NKMIIEEAKR SLHDALCVIR NLIRDNRVVY 430 440 450 460 470 480 GGGAAEISCA LAVSQEADKC PTLEQYAMRA FADALEVIPM ALSENSGMNP IQTMTEVRAR 490 500 510 520 530 540 QVKEMNPALG IDCLHKGTND MKQQHVIETL IGKKQQISLA TQMVRMILKI DDIRKPGESE E

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Prediction of the coding sequences of unidentified human genes. III. The coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by analysis of cDNA clones from human cell line KG-1." Nagase T., Miyajima N., Tanaka A., Sazuka T., Seki N., Sato S., Tabata S., Ishikawa K., Kawarabayasi Y., Kotani H., Nomura N. DNA Res. 2:37-43(1995) [PubMed: 7788527] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Bone marrow.
[2]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." 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. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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: Lung and Uterus.
[5]	Bienvenut W.V., Vousden K.H., Lukashchuk N. Submitted (MAR-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-24; 28-35; 50-59; 90-96; 133-170; 184-201; 203-214; 248-261; 264-275; 283-293; 324-340; 345-368; 382-388; 393-399; 401-410; 484-496; 514-525 AND 530-541, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, MASS SPECTROMETRY. Tissue: Lung carcinoma.
[6]	Bienvenut W.V., Waridel P., Quadroni M. Submitted (MAR-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-20; 97-126; 133-170; 184-201; 203-214; 266-275; 294-340; 345-368; 382-388 AND 401-410, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[7]	Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y. Submitted (DEC-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 203-210; 248-261; 324-340; 353-368 AND 515-525, MASS SPECTROMETRY. Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[8]	"A product of the human gene adjacent to parkin is a component of Lewy bodies and suppresses Pael receptor-induced cell death." Imai Y., Soda M., Murakami T., Shoji M., Abe K., Takahashi R. J. Biol. Chem. 278:51901-51910(2003) [PubMed: 14532270] [Abstract] Cited for: INTERACTION WITH PACRG.
[9]	"Transcriptomic and proteomic analyses of rhabdomyosarcoma cells reveal differential cellular gene expression in response to enterovirus 71 infection." Leong W.F., Chow V.T. Cell. Microbiol. 8:565-580(2006) [PubMed: 16548883] [Abstract] Cited for: INDUCTION, MASS SPECTROMETRY.
[10]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[11]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-223; LYS-232 AND LYS-399, MASS SPECTROMETRY.
[12]	"BBS6, BBS10, and BBS12 form a complex with CCT/TRiC family chaperonins and mediate BBSome assembly." Seo S., Baye L.M., Schulz N.P., Beck J.S., Zhang Q., Slusarski D.C., Sheffield V.C. Proc. Natl. Acad. Sci. U.S.A. 107:1488-1493(2010) [PubMed: 20080638] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN BBS/CCT COMPLEX.
[13]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]	"Mutation in the epsilon subunit of the cytosolic chaperonin-containing T-complex peptide-1 (Cct5) gene causes autosomal recessive mutilating sensory neuropathy with spastic paraplegia." Bouhouche A., Benomar A., Bouslam N., Chkili T., Yahyaoui M. J. Med. Genet. 43:441-443(2006) [PubMed: 16399879] [Abstract] Cited for: VARIANT HSNSP ARG-147.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D43950 mRNA. Translation: BAA07894.2. Different initiation. AK289353 mRNA. Translation: BAF82042.1. CH471102 Genomic DNA. Translation: EAX08072.1. BC006543 mRNA. Translation: AAH06543.1. BC035499 mRNA. Translation: AAH35499.1.
IPI	IPI00010720.
RefSeq	NP_036205.1. NM_012073.3.
UniGene	Hs.725167.
3D structure databases
ProteinModelPortal	P48643.
SMR	P48643. Positions 17-533.
ModBase	Search...
Protein-protein interaction databases
IntAct	P48643. 29 interactions.
MINT	MINT-1154718.
STRING	P48643.
PTM databases
PhosphoSite	P48643.
Polymorphism databases
DMDM	1351211.
2D gel databases
SWISS-2DPAGE	P48643.
OGP	P48643.
PHCI-2DPAGE	P48643.
REPRODUCTION-2DPAGE	IPI00010720.
Proteomic databases
PeptideAtlas	P48643.
PRIDE	P48643.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000280326; ENSP00000280326; ENSG00000150753.
GeneID	22948.
KEGG	hsa:22948.
UCSC	uc003jeq.1. human.
Organism-specific databases
CTD	22948.
GeneCards	GC05P010236.
H-InvDB	HIX0004744. HIX0120997.
HGNC	HGNC:1618. CCT5.
HPA	CAB006271. HPA002238. HPA005958.
MIM	256840. phenotype. 610150. gene.
neXtProt	NX_P48643.
Orphanet	2683. Sensory neuropathy - spastic paraplegia.
PharmGKB	PA26182.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG05593.
HOGENOM	HBG497503.
HOVERGEN	HBG106507.
InParanoid	P48643.
OMA	EYGRPFI.
OrthoDB	EOG40P46J.
PhylomeDB	P48643.
Enzyme and pathway databases
Reactome	REACT_17015. Metabolism of proteins.
Gene expression databases
ArrayExpress	P48643.
Bgee	P48643.
CleanEx	HS_CCT5.
Genevestigator	P48643.
GermOnline	ENSG00000150753. Homo sapiens.
Family and domain databases
InterPro	IPR012718. Chap_CCT_epsi. IPR017998. Chaperone_TCP-1. IPR002194. Chaperonin_TCP-1_CS. IPR002423. Cpn60/TCP-1. [Graphical view]
KO	K09497.
PANTHER	PTHR11353:SF25. Chap_CCT_epsi. 1 hit. PTHR11353. Cpn60/TCP-1. 1 hit.
Pfam	PF00118. Cpn60_TCP1. 1 hit. [Graphical view]
PRINTS	PR00304. TCOMPLEXTCP1.
SUPFAM	SSF48592. GroEL-ATPase. 1 hit.
TIGRFAMs	TIGR02343. Chap_CCT_epsi. 1 hit.
PROSITE	PS00750. TCP1_1. 1 hit. PS00751. TCP1_2. 1 hit. PS00995. TCP1_3. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	43711.
SOURCE	Search...

Entry information

Entry name

TCPE_HUMAN

Accession

Primary (citable) accession number: P48643
Secondary accession number(s): A8JZY8

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	February 1, 1996
Last modified:	December 14, 2011
This is version 120 of the entry and version 1 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.