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Protein

T-complex protein 1 subunit epsilon

Gene

CCT5

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • beta-tubulin binding Source: UniProtKB
  • G-protein beta-subunit binding Source: UniProtKB

GO - Biological processi

  • binding of sperm to zona pellucida Source: Ensembl
  • positive regulation of establishment of protein localization to telomere Source: BHF-UCL
  • positive regulation of protein localization to Cajal body Source: BHF-UCL
  • positive regulation of telomerase RNA localization to Cajal body Source: BHF-UCL
  • positive regulation of telomere maintenance via telomerase Source: BHF-UCL
  • protein folding Source: Reactome
  • protein stabilization Source: BHF-UCL
  • response to virus Source: UniProtKB
  • toxin transport Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-HSA-389957. Prefoldin mediated transfer of substrate to CCT/TriC.
R-HSA-389960. Formation of tubulin folding intermediates by CCT/TriC.
R-HSA-390450. Folding of actin by CCT/TriC.
R-HSA-390471. Association of TriC/CCT with target proteins during biosynthesis.
R-HSA-5620922. BBSome-mediated cargo-targeting to cilium.
R-HSA-6814122. Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.

Names & Taxonomyi

Protein namesi
Recommended name:
T-complex protein 1 subunit epsilon
Short name:
TCP-1-epsilon
Alternative name(s):
CCT-epsilon
Gene namesi
Name:CCT5
Synonyms:CCTE, KIAA0098
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:1618. CCT5.

Subcellular locationi

GO - Cellular componenti

  • cell body Source: Ensembl
  • centrosome Source: MGI
  • chaperonin-containing T-complex Source: UniProtKB
  • cytoplasm Source: HPA
  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • microtubule Source: UniProtKB
  • myelin sheath Source: Ensembl
  • nucleolus Source: HPA
  • zona pellucida receptor complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Involvement in diseasei

Neuropathy, hereditary sensory, with spastic paraplegia, autosomal recessive (HSNSP)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disease characterized by spastic paraplegia and progressive distal sensory neuropathy leading to mutilating ulcerations of the upper and lower limbs.
See also OMIM:256840
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti147 – 1471H → R in HSNSP. 1 Publication
VAR_030658

Keywords - Diseasei

Disease mutation, Neuropathy

Organism-specific databases

MalaCardsiCCT5.
MIMi256840. phenotype.
Orphaneti139578. Hereditary sensory and autonomic neuropathy with spastic paraplegia.
PharmGKBiPA26182.

Polymorphism and mutation databases

BioMutaiCCT5.
DMDMi1351211.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources2 Publications
Chaini2 – 541540T-complex protein 1 subunit epsilonPRO_0000128346Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources2 Publications
Modified residuei26 – 261PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP48643.
PaxDbiP48643.
PeptideAtlasiP48643.
PRIDEiP48643.

2D gel databases

OGPiP48643.
REPRODUCTION-2DPAGEIPI00010720.
SWISS-2DPAGEP48643.

PTM databases

iPTMnetiP48643.
PhosphoSiteiP48643.
SwissPalmiP48643.

Expressioni

Inductioni

Down-regulated in response to enterovirus 71 (EV71) infection (at protein level).1 Publication

Gene expression databases

BgeeiP48643.
CleanExiHS_CCT5.
ExpressionAtlasiP48643. baseline and differential.
GenevisibleiP48643. HS.

Organism-specific databases

HPAiCAB006271.
HPA002238.
HPA005958.

Interactioni

Subunit structurei

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. Interacts with DYX1C1 (By similarity).By similarity

GO - Molecular functioni

  • beta-tubulin binding Source: UniProtKB
  • G-protein beta-subunit binding Source: UniProtKB

Protein-protein interaction databases

BioGridi116603. 181 interactions.
DIPiDIP-31181N.
IntActiP48643. 100 interactions.
MINTiMINT-1154718.
STRINGi9606.ENSP00000280326.

Structurei

3D structure databases

ProteinModelPortaliP48643.
SMRiP48643. Positions 18-537.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the TCP-1 chaperonin family.Curated

Phylogenomic databases

eggNOGiKOG0357. Eukaryota.
COG0459. LUCA.
GeneTreeiENSGT00550000074988.
HOGENOMiHOG000226735.
HOVERGENiHBG106507.
InParanoidiP48643.
KOiK09497.
OMAiVDHEIAK.
OrthoDBiEOG722J8B.
PhylomeDBiP48643.
TreeFamiTF105638.

Family and domain databases

Gene3Di1.10.560.10. 2 hits.
3.30.260.10. 2 hits.
3.50.7.10. 1 hit.
InterProiIPR012718. Chap_CCT_epsi.
IPR017998. Chaperone_TCP-1.
IPR002194. Chaperonin_TCP-1_CS.
IPR002423. Cpn60/TCP-1.
IPR027409. GroEL-like_apical_dom.
IPR027413. GROEL-like_equatorial.
IPR027410. TCP-1-like_intermed.
[Graphical view]
PfamiPF00118. Cpn60_TCP1. 1 hit.
[Graphical view]
PRINTSiPR00304. TCOMPLEXTCP1.
SUPFAMiSSF52029. SSF52029. 1 hit.
TIGRFAMsiTIGR02343. chap_CCT_epsi. 1 hit.
PROSITEiPS00750. TCP1_1. 1 hit.
PS00751. TCP1_2. 1 hit.
PS00995. TCP1_3. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P48643-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MASMGTLAFD EYGRPFLIIK DQDRKSRLMG LEALKSHIMA AKAVANTMRT
60 70 80 90 100
SLGPNGLDKM MVDKDGDVTV TNDGATILSM MDVDHQIAKL MVELSKSQDD
110 120 130 140 150
EIGDGTTGVV VLAGALLEEA EQLLDRGIHP IRIADGYEQA ARVAIEHLDK
160 170 180 190 200
ISDSVLVDIK DTEPLIQTAK TTLGSKVVNS CHRQMAEIAV NAVLTVADME
210 220 230 240 250
RRDVDFELIK VEGKVGGRLE DTKLIKGVIV DKDFSHPQMP KKVEDAKIAI
260 270 280 290 300
LTCPFEPPKP KTKHKLDVTS VEDYKALQKY EKEKFEEMIQ QIKETGANLA
310 320 330 340 350
ICQWGFDDEA NHLLLQNNLP AVRWVGGPEI ELIAIATGGR IVPRFSELTA
360 370 380 390 400
EKLGFAGLVQ EISFGTTKDK MLVIEQCKNS RAVTIFIRGG NKMIIEEAKR
410 420 430 440 450
SLHDALCVIR NLIRDNRVVY GGGAAEISCA LAVSQEADKC PTLEQYAMRA
460 470 480 490 500
FADALEVIPM ALSENSGMNP IQTMTEVRAR QVKEMNPALG IDCLHKGTND
510 520 530 540
MKQQHVIETL IGKKQQISLA TQMVRMILKI DDIRKPGESE E
Length:541
Mass (Da):59,671
Last modified:February 1, 1996 - v1
Checksum:i164168BB80EF022A
GO
Isoform 2 (identifier: P48643-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-38: Missing.
     56-110: Missing.

Note: No experimental confirmation available.
Show »
Length:448
Mass (Da):49,526
Checksum:i9B4A960C92BF4327
GO

Sequence cautioni

The sequence BAA07894.2 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti55 – 551N → D in BAF83082 (PubMed:14702039).Curated
Sequence conflicti512 – 5121G → D in BAF83082 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti146 – 1461E → V.
Corresponds to variant rs11557652 [ dbSNP | Ensembl ].
VAR_052267
Natural varianti147 – 1471H → R in HSNSP. 1 Publication
VAR_030658

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3838Missing in isoform 2. 1 PublicationVSP_054005Add
BLAST
Alternative sequencei56 – 11055Missing in isoform 2. 1 PublicationVSP_054006Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D43950 mRNA. Translation: BAA07894.2. Different initiation.
AK289353 mRNA. Translation: BAF82042.1.
AK290393 mRNA. Translation: BAF83082.1.
AK302383 mRNA. Translation: BAG63700.1.
AC012640 Genomic DNA. No translation available.
CH471102 Genomic DNA. Translation: EAX08072.1.
BC006543 mRNA. Translation: AAH06543.1.
BC035499 mRNA. Translation: AAH35499.1.
CCDSiCCDS3877.1. [P48643-1]
RefSeqiNP_001293084.1. NM_001306155.1. [P48643-2]
NP_036205.1. NM_012073.4. [P48643-1]
UniGeneiHs.1600.
Hs.740762.

Genome annotation databases

EnsembliENST00000280326; ENSP00000280326; ENSG00000150753. [P48643-1]
ENST00000506600; ENSP00000423052; ENSG00000150753. [P48643-2]
GeneIDi22948.
KEGGihsa:22948.
UCSCiuc011cmt.3. human. [P48643-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D43950 mRNA. Translation: BAA07894.2. Different initiation.
AK289353 mRNA. Translation: BAF82042.1.
AK290393 mRNA. Translation: BAF83082.1.
AK302383 mRNA. Translation: BAG63700.1.
AC012640 Genomic DNA. No translation available.
CH471102 Genomic DNA. Translation: EAX08072.1.
BC006543 mRNA. Translation: AAH06543.1.
BC035499 mRNA. Translation: AAH35499.1.
CCDSiCCDS3877.1. [P48643-1]
RefSeqiNP_001293084.1. NM_001306155.1. [P48643-2]
NP_036205.1. NM_012073.4. [P48643-1]
UniGeneiHs.1600.
Hs.740762.

3D structure databases

ProteinModelPortaliP48643.
SMRiP48643. Positions 18-537.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116603. 181 interactions.
DIPiDIP-31181N.
IntActiP48643. 100 interactions.
MINTiMINT-1154718.
STRINGi9606.ENSP00000280326.

PTM databases

iPTMnetiP48643.
PhosphoSiteiP48643.
SwissPalmiP48643.

Polymorphism and mutation databases

BioMutaiCCT5.
DMDMi1351211.

2D gel databases

OGPiP48643.
REPRODUCTION-2DPAGEIPI00010720.
SWISS-2DPAGEP48643.

Proteomic databases

EPDiP48643.
PaxDbiP48643.
PeptideAtlasiP48643.
PRIDEiP48643.

Protocols and materials databases

DNASUi22948.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000280326; ENSP00000280326; ENSG00000150753. [P48643-1]
ENST00000506600; ENSP00000423052; ENSG00000150753. [P48643-2]
GeneIDi22948.
KEGGihsa:22948.
UCSCiuc011cmt.3. human. [P48643-1]

Organism-specific databases

CTDi22948.
GeneCardsiCCT5.
H-InvDBHIX0120997.
HGNCiHGNC:1618. CCT5.
HPAiCAB006271.
HPA002238.
HPA005958.
MalaCardsiCCT5.
MIMi256840. phenotype.
610150. gene.
neXtProtiNX_P48643.
Orphaneti139578. Hereditary sensory and autonomic neuropathy with spastic paraplegia.
PharmGKBiPA26182.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0357. Eukaryota.
COG0459. LUCA.
GeneTreeiENSGT00550000074988.
HOGENOMiHOG000226735.
HOVERGENiHBG106507.
InParanoidiP48643.
KOiK09497.
OMAiVDHEIAK.
OrthoDBiEOG722J8B.
PhylomeDBiP48643.
TreeFamiTF105638.

Enzyme and pathway databases

ReactomeiR-HSA-389957. Prefoldin mediated transfer of substrate to CCT/TriC.
R-HSA-389960. Formation of tubulin folding intermediates by CCT/TriC.
R-HSA-390450. Folding of actin by CCT/TriC.
R-HSA-390471. Association of TriC/CCT with target proteins during biosynthesis.
R-HSA-5620922. BBSome-mediated cargo-targeting to cilium.
R-HSA-6814122. Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.

Miscellaneous databases

ChiTaRSiCCT5. human.
GeneWikiiCCT5_(gene).
GenomeRNAii22948.
PROiP48643.
SOURCEiSearch...

Gene expression databases

BgeeiP48643.
CleanExiHS_CCT5.
ExpressionAtlasiP48643. baseline and differential.
GenevisibleiP48643. HS.

Family and domain databases

Gene3Di1.10.560.10. 2 hits.
3.30.260.10. 2 hits.
3.50.7.10. 1 hit.
InterProiIPR012718. Chap_CCT_epsi.
IPR017998. Chaperone_TCP-1.
IPR002194. Chaperonin_TCP-1_CS.
IPR002423. Cpn60/TCP-1.
IPR027409. GroEL-like_apical_dom.
IPR027413. GROEL-like_equatorial.
IPR027410. TCP-1-like_intermed.
[Graphical view]
PfamiPF00118. Cpn60_TCP1. 1 hit.
[Graphical view]
PRINTSiPR00304. TCOMPLEXTCP1.
SUPFAMiSSF52029. SSF52029. 1 hit.
TIGRFAMsiTIGR02343. chap_CCT_epsi. 1 hit.
PROSITEiPS00750. TCP1_1. 1 hit.
PS00751. TCP1_2. 1 hit.
PS00995. TCP1_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: Testis and Umbilical cord blood.
  3. "The DNA sequence and comparative analysis of human chromosome 5."
    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.
    Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Lung and Uterus.
  6. 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, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Lung carcinoma.
  7. 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, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryonic kidney.
  8. 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, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
  9. "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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PACRG.
  10. "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] [Europe PMC] [Abstract]
    Cited for: INDUCTION, IDENTIFICATION BY MASS SPECTROMETRY.
  11. "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] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN BBS/CCT COMPLEX.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  18. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "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] [Europe PMC] [Abstract]
    Cited for: VARIANT HSNSP ARG-147.

Entry informationi

Entry nameiTCPE_HUMAN
AccessioniPrimary (citable) accession number: P48643
Secondary accession number(s): A8JZY8, A8K2X8, B4DYD8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: June 8, 2016
This is version 166 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.