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P78371

- TCPB_HUMAN

UniProt

P78371 - TCPB_HUMAN

Protein

T-complex protein 1 subunit beta

Gene

CCT2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 141 (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. ATP binding Source: UniProtKB-KW
    2. protein binding Source: IntAct
    3. unfolded protein binding Source: UniProtKB

    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. chaperone-mediated protein complex assembly Source: MGI
    5. protein folding Source: UniProtKB

    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 beta
    Short name:
    TCP-1-beta
    Alternative name(s):
    CCT-beta
    Gene namesi
    Name:CCT2
    Synonyms:99D8.1, CCTB
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:1615. CCT2.

    Subcellular locationi

    Cytoplasm 1 Publication

    GO - Cellular componenti

    1. cell body Source: Ensembl
    2. chaperonin-containing T-complex Source: Ensembl
    3. cytosol Source: UniProtKB
    4. extracellular vesicular exosome Source: UniProt
    5. microtubule Source: UniProtKB
    6. zona pellucida receptor complex Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA26179.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed8 Publications
    Chaini2 – 535534T-complex protein 1 subunit betaPRO_0000128316Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine7 Publications
    Modified residuei3 – 31Phosphoserine2 Publications
    Modified residuei13 – 131N6-acetyllysine1 Publication
    Modified residuei154 – 1541N6-acetyllysine1 Publication
    Modified residuei181 – 1811N6-acetyllysine1 Publication
    Modified residuei260 – 2601Phosphoserine1 Publication
    Modified residuei261 – 2611Phosphothreonine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP78371.
    PaxDbiP78371.
    PeptideAtlasiP78371.
    PRIDEiP78371.

    2D gel databases

    OGPiP78371.
    REPRODUCTION-2DPAGEIPI00297779.
    SWISS-2DPAGEP78371.
    UCD-2DPAGEP78371.

    PTM databases

    PhosphoSiteiP78371.

    Expressioni

    Gene expression databases

    ArrayExpressiP78371.
    BgeeiP78371.
    CleanExiHS_CCT2.
    GenevestigatoriP78371.

    Organism-specific databases

    HPAiCAB009850.
    HPA003197.
    HPA003198.

    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 CCT8.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    BBS7Q8IWZ63EBI-357407,EBI-1806001

    Protein-protein interaction databases

    BioGridi115827. 106 interactions.
    DIPiDIP-38123N.
    IntActiP78371. 52 interactions.
    MINTiMINT-8213815.
    STRINGi9606.ENSP00000299300.

    Structurei

    3D structure databases

    ProteinModelPortaliP78371.
    SMRiP78371. Positions 14-526.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the TCP-1 chaperonin family.Curated

    Phylogenomic databases

    eggNOGiCOG0459.
    HOGENOMiHOG000226736.
    HOVERGENiHBG001052.
    InParanoidiP78371.
    KOiK09494.
    OMAiESGDNIR.
    OrthoDBiEOG7Q5HD3.
    PhylomeDBiP78371.
    TreeFamiTF105645.

    Family and domain databases

    Gene3Di1.10.560.10. 2 hits.
    3.30.260.10. 2 hits.
    3.50.7.10. 1 hit.
    InterProiIPR012716. Chap_CCT_beta.
    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.
    TIGRFAMsiTIGR02341. chap_CCT_beta. 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. Align

    Isoform 1 (identifier: P78371-1) [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

    MASLSLAPVN IFKAGADEER AETARLTSFI GAIAIGDLVK STLGPKGMDK    50
    ILLSSGRDAS LMVTNDGATI LKNIGVDNPA AKVLVDMSRV QDDEVGDGTT 100
    SVTVLAAELL REAESLIAKK IHPQTIIAGW REATKAAREA LLSSAVDHGS 150
    DEVKFRQDLM NIAGTTLSSK LLTHHKDHFT KLAVEAVLRL KGSGNLEAIH 200
    IIKKLGGSLA DSYLDEGFLL DKKIGVNQPK RIENAKILIA NTGMDTDKIK 250
    IFGSRVRVDS TAKVAEIEHA EKEKMKEKVE RILKHGINCF INRQLIYNYP 300
    EQLFGAAGVM AIEHADFAGV ERLALVTGGE IASTFDHPEL VKLGSCKLIE 350
    EVMIGEDKLI HFSGVALGEA CTIVLRGATQ QILDEAERSL HDALCVLAQT 400
    VKDSRTVYGG GCSEMLMAHA VTQLANRTPG KEAVAMESYA KALRMLPTII 450
    ADNAGYDSAD LVAQLRAAHS EGNTTAGLDM REGTIGDMAI LGITESFQVK 500
    RQVLLSAAEA AEVILRVDNI IKAAPRKRVP DHHPC 535
    Length:535
    Mass (Da):57,488
    Last modified:January 23, 2007 - v4
    Checksum:i57F9E1720D84A31F
    GO
    Isoform 2 (identifier: P78371-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-47: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:488
    Mass (Da):52,718
    Checksum:i5947D87827A365E3
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti51 – 511I → T in BAH11729. (PubMed:14702039)Curated
    Sequence conflicti126 – 1261I → T in CAG33352. 1 PublicationCurated
    Sequence conflicti354 – 3541I → T in BAF83456. (PubMed:14702039)Curated
    Sequence conflicti438 – 4381S → P in BAH13640. (PubMed:14702039)Curated
    Sequence conflicti444 – 4441R → K in BAG70037. (PubMed:19054851)Curated
    Sequence conflicti444 – 4441R → K in BAG70160. (PubMed:19054851)Curated
    Sequence conflicti504 – 5041L → P in CAG33352. 1 PublicationCurated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 4747Missing in isoform 2. 1 PublicationVSP_042648Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF026293 mRNA. Translation: AAC96012.1.
    AF026166 mRNA. Translation: AAC98906.1.
    BT019966 mRNA. Translation: AAV38769.1.
    AK290767 mRNA. Translation: BAF83456.1.
    AK294307 mRNA. Translation: BAH11729.1.
    AK302157 mRNA. Translation: BAH13640.1.
    AK316397 mRNA. Translation: BAH14768.1.
    AK316408 mRNA. Translation: BAH14779.1.
    CR457071 mRNA. Translation: CAG33352.1.
    AB451223 mRNA. Translation: BAG70037.1.
    AB451346 mRNA. Translation: BAG70160.1.
    AC018921 Genomic DNA. No translation available.
    CH471054 Genomic DNA. Translation: EAW97230.1.
    BC113514 mRNA. Translation: AAI13515.1.
    BC113516 mRNA. Translation: AAI13517.1.
    U91327 Genomic DNA. Translation: AAB67249.1.
    CCDSiCCDS55843.1. [P78371-2]
    CCDS8991.1. [P78371-1]
    RefSeqiNP_001185771.1. NM_001198842.1. [P78371-2]
    NP_006422.1. NM_006431.2. [P78371-1]
    UniGeneiHs.189772.

    Genome annotation databases

    EnsembliENST00000299300; ENSP00000299300; ENSG00000166226. [P78371-1]
    ENST00000543146; ENSP00000445471; ENSG00000166226. [P78371-2]
    GeneIDi10576.
    KEGGihsa:10576.
    UCSCiuc001svb.1. human. [P78371-1]

    Polymorphism databases

    DMDMi6094436.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF026293 mRNA. Translation: AAC96012.1 .
    AF026166 mRNA. Translation: AAC98906.1 .
    BT019966 mRNA. Translation: AAV38769.1 .
    AK290767 mRNA. Translation: BAF83456.1 .
    AK294307 mRNA. Translation: BAH11729.1 .
    AK302157 mRNA. Translation: BAH13640.1 .
    AK316397 mRNA. Translation: BAH14768.1 .
    AK316408 mRNA. Translation: BAH14779.1 .
    CR457071 mRNA. Translation: CAG33352.1 .
    AB451223 mRNA. Translation: BAG70037.1 .
    AB451346 mRNA. Translation: BAG70160.1 .
    AC018921 Genomic DNA. No translation available.
    CH471054 Genomic DNA. Translation: EAW97230.1 .
    BC113514 mRNA. Translation: AAI13515.1 .
    BC113516 mRNA. Translation: AAI13517.1 .
    U91327 Genomic DNA. Translation: AAB67249.1 .
    CCDSi CCDS55843.1. [P78371-2 ]
    CCDS8991.1. [P78371-1 ]
    RefSeqi NP_001185771.1. NM_001198842.1. [P78371-2 ]
    NP_006422.1. NM_006431.2. [P78371-1 ]
    UniGenei Hs.189772.

    3D structure databases

    ProteinModelPortali P78371.
    SMRi P78371. Positions 14-526.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115827. 106 interactions.
    DIPi DIP-38123N.
    IntActi P78371. 52 interactions.
    MINTi MINT-8213815.
    STRINGi 9606.ENSP00000299300.

    PTM databases

    PhosphoSitei P78371.

    Polymorphism databases

    DMDMi 6094436.

    2D gel databases

    OGPi P78371.
    REPRODUCTION-2DPAGE IPI00297779.
    SWISS-2DPAGE P78371.
    UCD-2DPAGE P78371.

    Proteomic databases

    MaxQBi P78371.
    PaxDbi P78371.
    PeptideAtlasi P78371.
    PRIDEi P78371.

    Protocols and materials databases

    DNASUi 10576.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000299300 ; ENSP00000299300 ; ENSG00000166226 . [P78371-1 ]
    ENST00000543146 ; ENSP00000445471 ; ENSG00000166226 . [P78371-2 ]
    GeneIDi 10576.
    KEGGi hsa:10576.
    UCSCi uc001svb.1. human. [P78371-1 ]

    Organism-specific databases

    CTDi 10576.
    GeneCardsi GC12P069979.
    HGNCi HGNC:1615. CCT2.
    HPAi CAB009850.
    HPA003197.
    HPA003198.
    MIMi 605139. gene.
    neXtProti NX_P78371.
    PharmGKBi PA26179.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0459.
    HOGENOMi HOG000226736.
    HOVERGENi HBG001052.
    InParanoidi P78371.
    KOi K09494.
    OMAi ESGDNIR.
    OrthoDBi EOG7Q5HD3.
    PhylomeDBi P78371.
    TreeFami TF105645.

    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 CCT2. human.
    GeneWikii CCT2_(gene).
    GenomeRNAii 10576.
    NextBioi 40141.
    PROi P78371.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P78371.
    Bgeei P78371.
    CleanExi HS_CCT2.
    Genevestigatori P78371.

    Family and domain databases

    Gene3Di 1.10.560.10. 2 hits.
    3.30.260.10. 2 hits.
    3.50.7.10. 1 hit.
    InterProi IPR012716. Chap_CCT_beta.
    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 TIGR02341. chap_CCT_beta. 1 hit.
    PROSITEi PS00750. TCP1_1. 1 hit.
    PS00751. TCP1_2. 1 hit.
    PS00995. TCP1_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Maturation of human cyclin E requires the function of eukaryotic chaperonin CCT."
      Won K.-A., Schumacher R.J., Farr G.W., Horwich A.L., Reed S.I.
      Mol. Cell. Biol. 18:7584-7589(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Isolation and expression of a human novel cDNA homologous to the beta subunit of mouse CCT (chaperonin-containing TCP-1)."
      Xin Y., Yu L., Bi A., Fan Y., Dai F., Zhang M., Zhang Q., Zhao S.
      Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    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 1 AND 2).
      Tissue: Amygdala and Testis.
    5. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    6. "Human protein factory for converting the transcriptome into an in vitro-expressed proteome."
      Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.
      , Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., Nomura N.
      Nat. Methods 5:1011-1017(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    7. "The finished DNA sequence of human chromosome 12."
      Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
      , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
      Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. "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: Brain.
    10. Adams M.D., Loftus B.J., Zhou L., Phillips C., Brandon R., Fuhrmann J., Kim U.J., Kerlavage A.R., Venter J.C.
      Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-217.
    11. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
      Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
      Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-20.
      Tissue: Platelet.
    12. Bienvenut W.V., Potts A., Quadroni M.
      Submitted (MAY-2004) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-13, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: B-cell lymphoma.
    13. Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 26-40; 58-72; 83-131; 139-154; 157-170; 182-189; 192-203; 205-222; 237-250; 285-342; 348-354; 359-402; 406-427; 432-441; 445-466; 482-500 AND 502-516, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
    14. "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.
    15. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "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 ALA-2; LYS-13; LYS-154 AND LYS-181, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "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.
    18. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3; SER-260 AND THR-261, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    22. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiTCPB_HUMAN
    AccessioniPrimary (citable) accession number: P78371
    Secondary accession number(s): A8K402
    , B5BTY7, B7Z243, B7Z7K4, B7ZAT2, Q14D36, Q6IAT3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 141 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 12
      Human chromosome 12: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3