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P49368

- TCPG_HUMAN

UniProt

P49368 - TCPG_HUMAN

Protein

T-complex protein 1 subunit gamma

Gene

CCT3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 152 (01 Oct 2014)
      Sequence version 4 (24 May 2005)
      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. ATP binding Source: UniProtKB-KW
    2. poly(A) RNA binding Source: UniProtKB
    3. protein binding Source: IntAct
    4. unfolded protein binding Source: ProtInc

    GO - Biological processi

    1. 'de novo' posttranslational protein folding Source: Reactome
    2. binding of sperm to zona pellucida Source: Ensembl
    3. cellular protein metabolic process Source: Reactome
    4. 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 gamma
    Short name:
    TCP-1-gamma
    Alternative name(s):
    CCT-gamma
    hTRiC5
    Gene namesi
    Name:CCT3
    Synonyms:CCTG, TRIC5
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:1616. CCT3.

    Subcellular locationi

    GO - Cellular componenti

    1. cell body Source: Ensembl
    2. chaperonin-containing T-complex Source: Ensembl
    3. cytoplasm Source: HPA
    4. cytoskeleton Source: ProtInc
    5. cytosol Source: Reactome
    6. extracellular vesicular exosome Source: UniProt
    7. microtubule Source: UniProtKB
    8. plasma membrane Source: HPA
    9. zona pellucida receptor complex Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA26180.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 545545T-complex protein 1 subunit gammaPRO_0000128321Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine2 Publications
    Modified residuei222 – 2221N6-acetyllysine1 Publication
    Modified residuei244 – 2441Phosphoserine1 Publication
    Modified residuei252 – 2521Phosphoserine1 Publication
    Disulfide bondi366 ↔ 372By similarity

    Keywords - PTMi

    Acetylation, Disulfide bond, Phosphoprotein

    Proteomic databases

    MaxQBiP49368.
    PaxDbiP49368.
    PRIDEiP49368.

    2D gel databases

    DOSAC-COBS-2DPAGEP49368.
    OGPiP49368.
    SWISS-2DPAGEP49368.

    PTM databases

    PhosphoSiteiP49368.

    Expressioni

    Gene expression databases

    ArrayExpressiP49368.
    BgeeiP49368.
    CleanExiHS_CCT3.
    GenevestigatoriP49368.

    Organism-specific databases

    HPAiHPA006543.

    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

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    RAF1P040493EBI-356673,EBI-365996

    Protein-protein interaction databases

    BioGridi113054. 99 interactions.
    DIPiDIP-32970N.
    IntActiP49368. 63 interactions.
    MINTiMINT-260598.
    STRINGi9606.ENSP00000357244.

    Structurei

    3D structure databases

    ProteinModelPortaliP49368.
    SMRiP49368. Positions 7-526.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the TCP-1 chaperonin family.Curated

    Phylogenomic databases

    eggNOGiCOG0459.
    HOGENOMiHOG000226732.
    HOVERGENiHBG104982.
    InParanoidiP49368.
    KOiK09495.
    OMAiTEMAVSH.
    OrthoDBiEOG7DJSKS.
    PhylomeDBiP49368.
    TreeFamiTF105649.

    Family and domain databases

    Gene3Di1.10.560.10. 2 hits.
    3.30.260.10. 2 hits.
    3.50.7.10. 1 hit.
    InterProiIPR012719. Chap_CCT_gamma.
    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.
    PTHR11353:SF63. PTHR11353:SF63. 1 hit.
    PfamiPF00118. Cpn60_TCP1. 1 hit.
    [Graphical view]
    PRINTSiPR00304. TCOMPLEXTCP1.
    SUPFAMiSSF48592. SSF48592. 2 hits.
    SSF52029. SSF52029. 1 hit.
    TIGRFAMsiTIGR02344. chap_CCT_gamma. 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.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P49368-1) [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

    MMGHRPVLVL SQNTKRESGR KVQSGNINAA KTIADIIRTC LGPKSMMKML    50
    LDPMGGIVMT NDGNAILREI QVQHPAAKSM IEISRTQDEE VGDGTTSVII 100
    LAGEMLSVAE HFLEQQMHPT VVISAYRKAL DDMISTLKKI SIPVDISDSD 150
    MMLNIINSSI TTKAISRWSS LACNIALDAV KMVQFEENGR KEIDIKKYAR 200
    VEKIPGGIIE DSCVLRGVMI NKDVTHPRMR RYIKNPRIVL LDSSLEYKKG 250
    ESQTDIEITR EEDFTRILQM EEEYIQQLCE DIIQLKPDVV ITEKGISDLA 300
    QHYLMRANIT AIRRVRKTDN NRIARACGAR IVSRPEELRE DDVGTGAGLL 350
    EIKKIGDEYF TFITDCKDPK ACTILLRGAS KEILSEVERN LQDAMQVCRN 400
    VLLDPQLVPG GGASEMAVAH ALTEKSKAMT GVEQWPYRAV AQALEVIPRT 450
    LIQNCGASTI RLLTSLRAKH TQENCETWGV NGETGTLVDM KELGIWEPLA 500
    VKLQTYKTAV ETAVLLLRID DIVSGHKKKG DDQSRQGGAP DAGQE 545
    Length:545
    Mass (Da):60,534
    Last modified:May 24, 2005 - v4
    Checksum:i0A528762EF24F36B
    GO
    Isoform 2 (identifier: P49368-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         32-69: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:507
    Mass (Da):56,431
    Checksum:i7A7F387DF6A76FFE
    GO

    Sequence cautioni

    The sequence AAH08019.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti251 – 2511E → G in CAA52808. (PubMed:8573069)Curated
    Sequence conflicti345 – 3451T → A in AAC50068. (PubMed:8001976)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti391 – 3911L → F.
    Corresponds to variant rs2230194 [ dbSNP | Ensembl ].
    VAR_052265

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei32 – 6938Missing in isoform 2. 1 PublicationVSP_042026Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK293477 mRNA. Translation: BAG56968.1.
    AL833197 mRNA. Translation: CAI46192.1.
    AL589685 Genomic DNA. Translation: CAI14167.1.
    BC006501 mRNA. Translation: AAH06501.3.
    BC008019 mRNA. Translation: AAH08019.1. Different initiation.
    X74801 mRNA. Translation: CAA52808.1.
    U17104 mRNA. Translation: AAC50068.1.
    CCDSiCCDS1140.2. [P49368-1]
    CCDS30888.1. [P49368-2]
    PIRiS61529. A38983.
    RefSeqiNP_001008800.1. NM_001008800.2. [P49368-2]
    NP_005989.3. NM_005998.4. [P49368-1]
    UniGeneiHs.491494.

    Genome annotation databases

    EnsembliENST00000295688; ENSP00000295688; ENSG00000163468. [P49368-1]
    ENST00000368259; ENSP00000357242; ENSG00000163468. [P49368-2]
    GeneIDi7203.
    KEGGihsa:7203.
    UCSCiuc001fol.2. human. [P49368-1]
    uc001fon.2. human. [P49368-2]

    Polymorphism databases

    DMDMi66774185.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK293477 mRNA. Translation: BAG56968.1 .
    AL833197 mRNA. Translation: CAI46192.1 .
    AL589685 Genomic DNA. Translation: CAI14167.1 .
    BC006501 mRNA. Translation: AAH06501.3 .
    BC008019 mRNA. Translation: AAH08019.1 . Different initiation.
    X74801 mRNA. Translation: CAA52808.1 .
    U17104 mRNA. Translation: AAC50068.1 .
    CCDSi CCDS1140.2. [P49368-1 ]
    CCDS30888.1. [P49368-2 ]
    PIRi S61529. A38983.
    RefSeqi NP_001008800.1. NM_001008800.2. [P49368-2 ]
    NP_005989.3. NM_005998.4. [P49368-1 ]
    UniGenei Hs.491494.

    3D structure databases

    ProteinModelPortali P49368.
    SMRi P49368. Positions 7-526.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113054. 99 interactions.
    DIPi DIP-32970N.
    IntActi P49368. 63 interactions.
    MINTi MINT-260598.
    STRINGi 9606.ENSP00000357244.

    PTM databases

    PhosphoSitei P49368.

    Polymorphism databases

    DMDMi 66774185.

    2D gel databases

    DOSAC-COBS-2DPAGE P49368.
    OGPi P49368.
    SWISS-2DPAGE P49368.

    Proteomic databases

    MaxQBi P49368.
    PaxDbi P49368.
    PRIDEi P49368.

    Protocols and materials databases

    DNASUi 7203.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000295688 ; ENSP00000295688 ; ENSG00000163468 . [P49368-1 ]
    ENST00000368259 ; ENSP00000357242 ; ENSG00000163468 . [P49368-2 ]
    GeneIDi 7203.
    KEGGi hsa:7203.
    UCSCi uc001fol.2. human. [P49368-1 ]
    uc001fon.2. human. [P49368-2 ]

    Organism-specific databases

    CTDi 7203.
    GeneCardsi GC01M156278.
    HGNCi HGNC:1616. CCT3.
    HPAi HPA006543.
    MIMi 600114. gene.
    neXtProti NX_P49368.
    PharmGKBi PA26180.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0459.
    HOGENOMi HOG000226732.
    HOVERGENi HBG104982.
    InParanoidi P49368.
    KOi K09495.
    OMAi TEMAVSH.
    OrthoDBi EOG7DJSKS.
    PhylomeDBi P49368.
    TreeFami TF105649.

    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 CCT3. human.
    GeneWikii CCT3.
    GenomeRNAii 7203.
    NextBioi 28226.
    PROi P49368.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P49368.
    Bgeei P49368.
    CleanExi HS_CCT3.
    Genevestigatori P49368.

    Family and domain databases

    Gene3Di 1.10.560.10. 2 hits.
    3.30.260.10. 2 hits.
    3.50.7.10. 1 hit.
    InterProi IPR012719. Chap_CCT_gamma.
    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.
    PTHR11353:SF63. PTHR11353:SF63. 1 hit.
    Pfami PF00118. Cpn60_TCP1. 1 hit.
    [Graphical view ]
    PRINTSi PR00304. TCOMPLEXTCP1.
    SUPFAMi SSF48592. SSF48592. 2 hits.
    SSF52029. SSF52029. 1 hit.
    TIGRFAMsi TIGR02344. chap_CCT_gamma. 1 hit.
    PROSITEi PS00750. TCP1_1. 1 hit.
    PS00751. TCP1_2. 1 hit.
    PS00995. TCP1_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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] (ISOFORM 2).
      Tissue: Cerebellum.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Lymph node.
    3. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Lung.
    5. Bienvenut W.V., Boldt K., von Kriegsheim A.F., Kolch W.
      Submitted (JUL-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 1-15; 32-38; 49-85; 129-138; 182-191; 238-248; 295-306; 382-389; 428-449 AND 508-528, ACETYLATION AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Hepatoma.
    6. "Cloning, structure and mRNA expression of human Cctg, which encodes the chaperonin subunit CCT gamma."
      Walkley N.A., Demaine A.G., Malik A.N.
      Biochem. J. 313:381-389(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2-545.
      Tissue: Kidney.
    7. Lubec G., Vishwanath V.
      Submitted (MAR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 204-216; 331-353 AND 508-518, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Brain and Cajal-Retzius cell.
    8. "Assignment of the human homologue of the mTRiC-P5 gene (TRIC5) to band 1q23 by fluorescence in situ hybridization."
      Sevigny G., Joly E., Bibor-Hardy V., Lemieux N.
      Genomics 22:634-636(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 345-544.
    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. "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 MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "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-244, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    12. "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-222, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "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, IDENTIFICATION IN BBS/CCT COMPLEX.
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "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-252, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiTCPG_HUMAN
    AccessioniPrimary (citable) accession number: P49368
    Secondary accession number(s): A6NE14, Q5SZY1, Q9BR64
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: May 24, 2005
    Last modified: October 1, 2014
    This is version 152 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 1
      Human chromosome 1: 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

    External Data

    Dasty 3