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P50990 - TCPQ_HUMAN

UniProt

P50990 - TCPQ_HUMAN

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Protein

T-complex protein 1 subunit theta

Gene

CCT8

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

  1. ATPase activity, coupled Source: ProtInc
  2. ATP binding Source: UniProtKB-KW

GO - Biological processi

  1. 'de novo' posttranslational protein folding Source: Reactome
  2. ATP catabolic process Source: GOC
  3. binding of sperm to zona pellucida Source: Ensembl
  4. cellular protein metabolic process Source: Reactome
  5. protein folding Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_16907. Association of TriC/CCT with target proteins during biosynthesis.
REACT_16936. Prefoldin mediated transfer of substrate to CCT/TriC.
REACT_16956. Formation of tubulin folding intermediates by CCT/TriC.
REACT_17050. Folding of actin by CCT/TriC.

Names & Taxonomyi

Protein namesi
Recommended name:
T-complex protein 1 subunit theta
Short name:
TCP-1-theta
Alternative name(s):
CCT-theta
Renal carcinoma antigen NY-REN-15
Gene namesi
Name:CCT8
Synonyms:C21orf112, CCTQ, KIAA0002
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
ProteomesiUP000005640: Chromosome 21

Organism-specific databases

HGNCiHGNC:1623. CCT8.

Subcellular locationi

Cytoplasm 1 Publication. Cytoplasm › cytoskeleton › microtubule organizing center › centrosome 1 Publication

GO - Cellular componenti

  1. aggresome Source: HPA
  2. cell body Source: Ensembl
  3. centrosome Source: MGI
  4. chaperonin-containing T-complex Source: Ensembl
  5. cytoplasm Source: HPA
  6. cytosol Source: UniProtKB
  7. extracellular vesicular exosome Source: UniProtKB
  8. intermediate filament cytoskeleton Source: HPA
  9. microtubule Source: UniProtKB
  10. zona pellucida receptor complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26186.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 548547T-complex protein 1 subunit thetaPRO_0000128373Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei23 – 231Phosphoserine2 Publications
Modified residuei30 – 301Phosphotyrosine1 Publication
Cross-linki225 – 225Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki235 – 235Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei318 – 3181N6-acetyllysine1 Publication
Modified residuei400 – 4001N6-acetyllysine1 Publication
Modified residuei466 – 4661N6-acetyllysine1 Publication
Modified residuei505 – 5051Phosphotyrosine1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP50990.
PaxDbiP50990.
PRIDEiP50990.

2D gel databases

OGPiP50990.
REPRODUCTION-2DPAGEIPI00784090.
P50990.

PTM databases

PhosphoSiteiP50990.

Expressioni

Gene expression databases

BgeeiP50990.
CleanExiHS_CCT8.
ExpressionAtlasiP50990. baseline and differential.
GenevestigatoriP50990.

Organism-specific databases

HPAiHPA018520.
HPA021051.
HPA029426.

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

Protein-protein interaction databases

BioGridi115933. 93 interactions.
DIPiDIP-38124N.
IntActiP50990. 40 interactions.
MINTiMINT-1152593.
STRINGi9606.ENSP00000286788.

Structurei

3D structure databases

ProteinModelPortaliP50990.
SMRiP50990. Positions 13-528.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the TCP-1 chaperonin family.Curated

Phylogenomic databases

eggNOGiCOG0459.
GeneTreeiENSGT00550000074783.
HOGENOMiHOG000226734.
HOVERGENiHBG103107.
InParanoidiP50990.
KOiK09500.
OMAiKDWDDDQ.
OrthoDBiEOG7JQBN8.
PhylomeDBiP50990.
TreeFamiTF105699.

Family and domain databases

Gene3Di1.10.560.10. 2 hits.
3.30.260.10. 2 hits.
3.50.7.10. 1 hit.
InterProiIPR012721. Chap_CCT_theta.
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]
PANTHERiPTHR11353. PTHR11353. 1 hit.
PfamiPF00118. Cpn60_TCP1. 1 hit.
[Graphical view]
PRINTSiPR00304. TCOMPLEXTCP1.
SUPFAMiSSF48592. SSF48592. 2 hits.
SSF52029. SSF52029. 1 hit.
TIGRFAMsiTIGR02346. chap_CCT_theta. 1 hit.
PROSITEiPS00750. TCP1_1. 1 hit.
PS00751. TCP1_2. 1 hit.
PS00995. TCP1_3. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P50990-1) [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
MALHVPKAPG FAQMLKEGAK HFSGLEEAVY RNIQACKELA QTTRTAYGPN 
        60         70         80         90        100
GMNKMVINHL EKLFVTNDAA TILRELEVQH PAAKMIVMAS HMQEQEVGDG 
       110        120        130        140        150
TNFVLVFAGA LLELAEELLR IGLSVSEVIE GYEIACRKAH EILPNLVCCS 
       160        170        180        190        200
AKNLRDIDEV SSLLRTSIMS KQYGNEVFLA KLIAQACVSI FPDSGHFNVD 
       210        220        230        240        250
NIRVCKILGS GISSSSVLHG MVFKKETEGD VTSVKDAKIA VYSCPFDGMI 
       260        270        280        290        300
TETKGTVLIK TAEELMNFSK GEENLMDAQV KAIADTGANV VVTGGKVADM 
       310        320        330        340        350
ALHYANKYNI MLVRLNSKWD LRRLCKTVGA TALPRLTPPV LEEMGHCDSV 
       360        370        380        390        400
YLSEVGDTQV VVFKHEKEDG AISTIVLRGS TDNLMDDIER AVDDGVNTFK 
       410        420        430        440        450
VLTRDKRLVP GGGATEIELA KQITSYGETC PGLEQYAIKK FAEAFEAIPR 
       460        470        480        490        500
ALAENSGVKA NEVISKLYAV HQEGNKNVGL DIEAEVPAVK DMLEAGILDT 
       510        520        530        540 
YLGKYWAIKL ATNAAVTVLR VDQIIMAKPA GGPKPPSGKK DWDDDQND
Length:548
Mass (Da):59,621
Last modified:January 23, 2007 - v4
Checksum:i566A6622BC2D15E9
GO
Isoform 2 (identifier: P50990-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-20: MALHVPKAPGFAQMLKEGAK → M

Note: No experimental confirmation available.

Show »
Length:529
Mass (Da):57,645
Checksum:i7468208B8A3B84E2
GO
Isoform 3 (identifier: P50990-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-78: MALHVPKAPG...AATILRELEV → MDQMV

Note: No experimental confirmation available.

Show »
Length:475
Mass (Da):51,586
Checksum:i2D97E8F445125063
GO

Sequence cautioni

The sequence BAA02792.2 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti50 – 501N → K(PubMed:7584026)Curated
Sequence conflicti50 – 501N → K(PubMed:8590283)Curated
Sequence conflicti391 – 3911A → V in BAA02792. (PubMed:7584026)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti4 – 41H → Q.
Corresponds to variant rs16983693 [ dbSNP | Ensembl ].		VAR_052270
Natural varianti409 – 4091V → I.
Corresponds to variant rs8129954 [ dbSNP | Ensembl ].		VAR_052271

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 7878MALHV…RELEV → MDQMV in isoform 3. 1 PublicationVSP_054691Add
BLAST
Alternative sequencei1 – 2020MALHV…KEGAK → M in isoform 2. 1 PublicationVSP_054692Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D13627 mRNA. Translation: BAA02792.2. Different initiation.
D42052 Genomic DNA. Translation: BAA07652.1. Sequence problems.
AF129075 Genomic DNA. No translation available.
AK293705 mRNA. Translation: BAG57138.1.
AK298801 mRNA. Translation: BAG60936.1.
AL163249 Genomic DNA. Translation: CAB90433.1.
BC072001 mRNA. Translation: AAH72001.1.
BC095470 mRNA. Translation: AAH95470.1.
Z37163 mRNA. Translation: CAA85520.1.
CCDSiCCDS33528.1. [P50990-1]
CCDS68180.1. [P50990-3]
PIRiPC4021.
RefSeqiNP_001269836.1. NM_001282907.1. [P50990-2]
NP_001269838.1. NM_001282909.1. [P50990-3]
NP_006576.2. NM_006585.3. [P50990-1]
UniGeneiHs.125113.

Genome annotation databases

EnsembliENST00000286788; ENSP00000286788; ENSG00000156261. [P50990-1]
ENST00000540844; ENSP00000442730; ENSG00000156261. [P50990-3]
GeneIDi10694.
KEGGihsa:10694.
UCSCiuc002yna.3. human. [P50990-1]

Polymorphism databases

DMDMi9988062.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D13627 mRNA. Translation: BAA02792.2. Different initiation.
D42052 Genomic DNA. Translation: BAA07652.1. Sequence problems.
AF129075 Genomic DNA. No translation available.
AK293705 mRNA. Translation: BAG57138.1.
AK298801 mRNA. Translation: BAG60936.1.
AL163249 Genomic DNA. Translation: CAB90433.1.
BC072001 mRNA. Translation: AAH72001.1.
BC095470 mRNA. Translation: AAH95470.1.
Z37163 mRNA. Translation: CAA85520.1.
CCDSiCCDS33528.1. [P50990-1]
CCDS68180.1. [P50990-3]
PIRiPC4021.
RefSeqiNP_001269836.1. NM_001282907.1. [P50990-2]
NP_001269838.1. NM_001282909.1. [P50990-3]
NP_006576.2. NM_006585.3. [P50990-1]
UniGeneiHs.125113.

3D structure databases

ProteinModelPortaliP50990.
SMRiP50990. Positions 13-528.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115933. 93 interactions.
DIPiDIP-38124N.
IntActiP50990. 40 interactions.
MINTiMINT-1152593.
STRINGi9606.ENSP00000286788.

PTM databases

PhosphoSiteiP50990.

Polymorphism databases

DMDMi9988062.

2D gel databases

OGPiP50990.
REPRODUCTION-2DPAGEIPI00784090.
P50990.

Proteomic databases

MaxQBiP50990.
PaxDbiP50990.
PRIDEiP50990.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000286788; ENSP00000286788; ENSG00000156261. [P50990-1]
ENST00000540844; ENSP00000442730; ENSG00000156261. [P50990-3]
GeneIDi10694.
KEGGihsa:10694.
UCSCiuc002yna.3. human. [P50990-1]

Organism-specific databases

CTDi10694.
GeneCardsiGC21M030428.
HGNCiHGNC:1623. CCT8.
HPAiHPA018520.
HPA021051.
HPA029426.
neXtProtiNX_P50990.
PharmGKBiPA26186.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0459.
GeneTreeiENSGT00550000074783.
HOGENOMiHOG000226734.
HOVERGENiHBG103107.
InParanoidiP50990.
KOiK09500.
OMAiKDWDDDQ.
OrthoDBiEOG7JQBN8.
PhylomeDBiP50990.
TreeFamiTF105699.

Enzyme and pathway databases

ReactomeiREACT_16907. Association of TriC/CCT with target proteins during biosynthesis.
REACT_16936. Prefoldin mediated transfer of substrate to CCT/TriC.
REACT_16956. Formation of tubulin folding intermediates by CCT/TriC.
REACT_17050. Folding of actin by CCT/TriC.

Miscellaneous databases

ChiTaRSiCCT8. human.
GeneWikiiCCT8.
GenomeRNAii10694.
NextBioi35471264.
PROiP50990.

Gene expression databases

BgeeiP50990.
CleanExiHS_CCT8.
ExpressionAtlasiP50990. baseline and differential.
GenevestigatoriP50990.

Family and domain databases

Gene3Di1.10.560.10. 2 hits.
3.30.260.10. 2 hits.
3.50.7.10. 1 hit.
InterProiIPR012721. Chap_CCT_theta.
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]
PANTHERiPTHR11353. PTHR11353. 1 hit.
PfamiPF00118. Cpn60_TCP1. 1 hit.
[Graphical view]
PRINTSiPR00304. TCOMPLEXTCP1.
SUPFAMiSSF48592. SSF48592. 2 hits.
SSF52029. SSF52029. 1 hit.
TIGRFAMsiTIGR02346. chap_CCT_theta. 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. I. The coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of randomly sampled cDNA clones from human immature myeloid cell line KG-1."
    Nomura N., Miyajima N., Sazuka T., Tanaka A., Kawarabayasi Y., Sato S., Nagase T., Seki N., Ishikawa K., Tabata S.
    DNA Res. 1:27-35(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Bone marrow.
  2. "Nucleotide sequence surrounding the locus marker D21S246 on human chromosome 21."
    Yamazaki M., Ono A., Watanabe K., Sasaki K., Tashiro H., Nomura T.
    DNA Res. 2:187-189(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. Taudien S., Dagand E., Delabar J., Nordsiek G., Drescher B., Weber J., Schattevoy R., Menzel U., Yaspo M.-L., Rosenthal A.
    Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "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 2 AND 3).
    Tissue: Cerebellum.
  5. "The DNA sequence of human chromosome 21."
    Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A.
    , Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.
    Nature 405:311-319(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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: Chondrosarcoma and Liver.
  7. Bienvenut W.V.
    Submitted (OCT-2004) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-16; 55-74; 156-165; 172-181; 283-296; 408-421; 441-450 AND 510-520, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: B-cell lymphoma.
  8. "The eighth Cct gene, Cctq, encoding the theta subunit of the cytosolic chaperonin containing TCP-1."
    Kubota H., Hynes G., Willison K.
    Gene 154:231-236(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 33-65 (ISOFORM 1/2).
  9. Cited for: IDENTIFICATION AS A RENAL CANCER ANTIGEN.
    Tissue: Renal cell carcinoma.
  10. "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.
  11. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
    Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
    Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-505, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Tryptic digestion of ubiquitin standards reveals an improved strategy for identifying ubiquitinated proteins by mass spectrometry."
    Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.
    Proteomics 7:868-874(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-225 AND LYS-235.
    Tissue: Mammary cancer.
  13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23 AND TYR-30, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  15. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-318; LYS-400 AND LYS-466, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "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.
  17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Entry informationi

Entry nameiTCPQ_HUMAN
AccessioniPrimary (citable) accession number: P50990
Secondary accession number(s): A6NN54
, B4DEM7, B4DQH4, Q4VBP8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2007
Last modified: January 7, 2015
This is version 148 of the entry and version 4 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 21
    Human chromosome 21: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.