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P50990

- TCPQ_HUMAN

UniProt

P50990 - TCPQ_HUMAN

Protein

T-complex protein 1 subunit theta

Gene

CCT8

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 146 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      Previous versions | rss
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    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

    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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 21

    Organism-specific databases

    HGNCiHGNC:1623. CCT8.

    Subcellular locationi

    Cytoplasm 1 Publication. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome 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: UniProt
    8. intermediate filament cytoskeleton Source: HPA
    9. microtubule Source: UniProtKB
    10. zona pellucida receptor complex Source: Ensembl

    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

    ArrayExpressiP50990.
    BgeeiP50990.
    CleanExiHS_CCT8.
    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. 83 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.
    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

    MALHVPKAPG FAQMLKEGAK HFSGLEEAVY RNIQACKELA QTTRTAYGPN    50
    GMNKMVINHL EKLFVTNDAA TILRELEVQH PAAKMIVMAS HMQEQEVGDG 100
    TNFVLVFAGA LLELAEELLR IGLSVSEVIE GYEIACRKAH EILPNLVCCS 150
    AKNLRDIDEV SSLLRTSIMS KQYGNEVFLA KLIAQACVSI FPDSGHFNVD 200
    NIRVCKILGS GISSSSVLHG MVFKKETEGD VTSVKDAKIA VYSCPFDGMI 250
    TETKGTVLIK TAEELMNFSK GEENLMDAQV KAIADTGANV VVTGGKVADM 300
    ALHYANKYNI MLVRLNSKWD LRRLCKTVGA TALPRLTPPV LEEMGHCDSV 350
    YLSEVGDTQV VVFKHEKEDG AISTIVLRGS TDNLMDDIER AVDDGVNTFK 400
    VLTRDKRLVP GGGATEIELA KQITSYGETC PGLEQYAIKK FAEAFEAIPR 450
    ALAENSGVKA NEVISKLYAV HQEGNKNVGL DIEAEVPAVK DMLEAGILDT 500
    YLGKYWAIKL ATNAAVTVLR VDQIIMAKPA GGPKPPSGKK DWDDDQND 548
    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.

    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:
    EMBL
    GenBank
    DDBJ
    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]
    CCDS68181.1. [P50990-2]
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS33528.1. [P50990-1 ]
    CCDS68180.1. [P50990-3 ]
    CCDS68181.1. [P50990-2 ]
    PIRi PC4021.
    RefSeqi NP_001269836.1. NM_001282907.1. [P50990-2 ]
    NP_001269838.1. NM_001282909.1. [P50990-3 ]
    NP_006576.2. NM_006585.3. [P50990-1 ]
    UniGenei Hs.125113.

    3D structure databases

    ProteinModelPortali P50990.
    SMRi P50990. Positions 13-528.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115933. 83 interactions.
    DIPi DIP-38124N.
    IntActi P50990. 40 interactions.
    MINTi MINT-1152593.
    STRINGi 9606.ENSP00000286788.

    PTM databases

    PhosphoSitei P50990.

    Polymorphism databases

    DMDMi 9988062.

    2D gel databases

    OGPi P50990.
    REPRODUCTION-2DPAGE IPI00784090.
    P50990.

    Proteomic databases

    MaxQBi P50990.
    PaxDbi P50990.
    PRIDEi P50990.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000286788 ; ENSP00000286788 ; ENSG00000156261 . [P50990-1 ]
    ENST00000540844 ; ENSP00000442730 ; ENSG00000156261 . [P50990-3 ]
    GeneIDi 10694.
    KEGGi hsa:10694.
    UCSCi uc002yna.3. human. [P50990-1 ]

    Organism-specific databases

    CTDi 10694.
    GeneCardsi GC21M030428.
    HGNCi HGNC:1623. CCT8.
    HPAi HPA018520.
    HPA021051.
    HPA029426.
    neXtProti NX_P50990.
    PharmGKBi PA26186.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0459.
    HOGENOMi HOG000226734.
    HOVERGENi HBG103107.
    InParanoidi P50990.
    KOi K09500.
    OMAi KDWDDDQ.
    OrthoDBi EOG7JQBN8.
    PhylomeDBi P50990.
    TreeFami TF105699.

    Enzyme and pathway databases

    Reactomei REACT_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

    ChiTaRSi CCT8. human.
    GeneWikii CCT8.
    GenomeRNAii 10694.
    NextBioi 35471264.
    PROi P50990.

    Gene expression databases

    ArrayExpressi P50990.
    Bgeei P50990.
    CleanExi HS_CCT8.
    Genevestigatori P50990.

    Family and domain databases

    Gene3Di 1.10.560.10. 2 hits.
    3.30.260.10. 2 hits.
    3.50.7.10. 1 hit.
    InterProi IPR012721. 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 ]
    PANTHERi PTHR11353. PTHR11353. 1 hit.
    Pfami PF00118. Cpn60_TCP1. 1 hit.
    [Graphical view ]
    PRINTSi PR00304. TCOMPLEXTCP1.
    SUPFAMi SSF48592. SSF48592. 2 hits.
    SSF52029. SSF52029. 1 hit.
    TIGRFAMsi TIGR02346. chap_CCT_theta. 1 hit.
    PROSITEi PS00750. TCP1_1. 1 hit.
    PS00751. TCP1_2. 1 hit.
    PS00995. TCP1_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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].

    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: October 1, 2014
    This is version 146 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