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P50991

- TCPD_HUMAN

UniProt

P50991 - TCPD_HUMAN

Protein

T-complex protein 1 subunit delta

Gene

CCT4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 140 (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. 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 delta
    Short name:
    TCP-1-delta
    Alternative name(s):
    CCT-delta
    Stimulator of TAR RNA-binding
    Gene namesi
    Name:CCT4
    Synonyms:CCTD, SRB
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:1617. CCT4.

    Subcellular locationi

    Cytoplasm. Melanosome. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome
    Note: Identified by mass spectrometry in melanosome fractions from stage I to stage IV.

    GO - Cellular componenti

    1. cell body Source: Ensembl
    2. centrosome Source: MGI
    3. chaperonin-containing T-complex Source: Ensembl
    4. cytoplasm Source: HPA
    5. cytosol Source: Reactome
    6. extracellular vesicular exosome Source: UniProt
    7. melanosome Source: UniProtKB-SubCell
    8. microtubule Source: UniProtKB
    9. nucleus Source: HPA
    10. zona pellucida receptor complex Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA26181.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 539538T-complex protein 1 subunit deltaPRO_0000128332Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei21 – 211N6-acetyllysineBy similarity
    Modified residuei288 – 2881N6-acetyllysine1 Publication
    Modified residuei302 – 3021N6-acetyllysine1 Publication
    Modified residuei319 – 3191N6-acetyllysine1 Publication
    Modified residuei326 – 3261N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP50991.
    PaxDbiP50991.
    PeptideAtlasiP50991.
    PRIDEiP50991.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00302927.
    UCD-2DPAGEP50991.

    PTM databases

    PhosphoSiteiP50991.

    Miscellaneous databases

    PMAP-CutDBP50991.

    Expressioni

    Gene expression databases

    ArrayExpressiP50991.
    BgeeiP50991.
    CleanExiHS_CCT4.
    GenevestigatoriP50991.

    Organism-specific databases

    HPAiHPA029349.

    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
    OLR1P783803EBI-356876,EBI-7151999

    Protein-protein interaction databases

    BioGridi115826. 84 interactions.
    DIPiDIP-32971N.
    IntActiP50991. 46 interactions.
    MINTiMINT-1157924.
    STRINGi9606.ENSP00000377958.

    Structurei

    3D structure databases

    ProteinModelPortaliP50991.
    SMRiP50991. Positions 18-539.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the TCP-1 chaperonin family.Curated

    Phylogenomic databases

    eggNOGiCOG0459.
    HOGENOMiHOG000226735.
    HOVERGENiHBG106507.
    InParanoidiP50991.
    KOiK09496.
    OMAiPCAKMLV.
    OrthoDBiEOG722J8B.
    PhylomeDBiP50991.
    TreeFamiTF106332.

    Family and domain databases

    Gene3Di1.10.560.10. 2 hits.
    3.30.260.10. 2 hits.
    3.50.7.10. 1 hit.
    InterProiIPR012717. Chap_CCT_delta.
    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.
    TIGRFAMsiTIGR02342. chap_CCT_delta. 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: P50991-1) [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

    MPENVAPRSG ATAGAAGGRG KGAYQDRDKP AQIRFSNISA AKAVADAIRT    50
    SLGPKGMDKM IQDGKGDVTI TNDGATILKQ MQVLHPAARM LVELSKAQDI 100
    EAGDGTTSVV IIAGSLLDSC TKLLQKGIHP TIISESFQKA LEKGIEILTD 150
    MSRPVELSDR ETLLNSATTS LNSKVVSQYS SLLSPMSVNA VMKVIDPATA 200
    TSVDLRDIKI VKKLGGTIDD CELVEGLVLT QKVSNSGITR VEKAKIGLIQ 250
    FCLSAPKTDM DNQIVVSDYA QMDRVLREER AYILNLVKQI KKTGCNVLLI 300
    QKSILRDALS DLALHFLNKM KIMVIKDIER EDIEFICKTI GTKPVAHIDQ 350
    FTADMLGSAE LAEEVNLNGS GKLLKITGCA SPGKTVTIVV RGSNKLVIEE 400
    AERSIHDALC VIRCLVKKRA LIAGGGAPEI ELALRLTEYS RTLSGMESYC 450
    VRAFADAMEV IPSTLAENAG LNPISTVTEL RNRHAQGEKT AGINVRKGGI 500
    SNILEELVVQ PLLVSVSALT LATETVRSIL KIDDVVNTR 539
    Length:539
    Mass (Da):57,924
    Last modified:January 23, 2007 - v4
    Checksum:i39913C0D0735180D
    GO
    Isoform 2 (identifier: P50991-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         60-89: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:509
    Mass (Da):54,720
    Checksum:i53EDE4CD2799D28B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti435 – 4351R → A in AAC50384. (PubMed:8626763)Curated
    Sequence conflicti531 – 5311K → R in BAH13897. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti112 – 1121I → V.
    Corresponds to variant rs2272428 [ dbSNP | Ensembl ].
    VAR_052266

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei60 – 8930Missing in isoform 2. 1 PublicationVSP_045537Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U38846 mRNA. Translation: AAC50384.1.
    AF026291 mRNA. Translation: AAC96010.1.
    AK303082 mRNA. Translation: BAH13897.1.
    AK312586 mRNA. Translation: BAG35480.1.
    AC107081 Genomic DNA. Translation: AAY24140.1.
    BC014676 mRNA. Translation: AAH14676.1.
    BC106934 mRNA. Translation: AAI06935.1.
    BC106933 mRNA. Translation: AAI06934.1.
    CCDSiCCDS33206.1. [P50991-1]
    CCDS58711.1. [P50991-2]
    RefSeqiNP_001243650.1. NM_001256721.1. [P50991-2]
    NP_006421.2. NM_006430.3. [P50991-1]
    UniGeneiHs.421509.

    Genome annotation databases

    EnsembliENST00000394440; ENSP00000377958; ENSG00000115484. [P50991-1]
    ENST00000544079; ENSP00000443061; ENSG00000115484. [P50991-2]
    GeneIDi10575.
    KEGGihsa:10575.
    UCSCiuc002sbo.4. human. [P50991-1]

    Polymorphism databases

    DMDMi52001478.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U38846 mRNA. Translation: AAC50384.1 .
    AF026291 mRNA. Translation: AAC96010.1 .
    AK303082 mRNA. Translation: BAH13897.1 .
    AK312586 mRNA. Translation: BAG35480.1 .
    AC107081 Genomic DNA. Translation: AAY24140.1 .
    BC014676 mRNA. Translation: AAH14676.1 .
    BC106934 mRNA. Translation: AAI06935.1 .
    BC106933 mRNA. Translation: AAI06934.1 .
    CCDSi CCDS33206.1. [P50991-1 ]
    CCDS58711.1. [P50991-2 ]
    RefSeqi NP_001243650.1. NM_001256721.1. [P50991-2 ]
    NP_006421.2. NM_006430.3. [P50991-1 ]
    UniGenei Hs.421509.

    3D structure databases

    ProteinModelPortali P50991.
    SMRi P50991. Positions 18-539.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115826. 84 interactions.
    DIPi DIP-32971N.
    IntActi P50991. 46 interactions.
    MINTi MINT-1157924.
    STRINGi 9606.ENSP00000377958.

    PTM databases

    PhosphoSitei P50991.

    Polymorphism databases

    DMDMi 52001478.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00302927.
    UCD-2DPAGE P50991.

    Proteomic databases

    MaxQBi P50991.
    PaxDbi P50991.
    PeptideAtlasi P50991.
    PRIDEi P50991.

    Protocols and materials databases

    DNASUi 10575.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000394440 ; ENSP00000377958 ; ENSG00000115484 . [P50991-1 ]
    ENST00000544079 ; ENSP00000443061 ; ENSG00000115484 . [P50991-2 ]
    GeneIDi 10575.
    KEGGi hsa:10575.
    UCSCi uc002sbo.4. human. [P50991-1 ]

    Organism-specific databases

    CTDi 10575.
    GeneCardsi GC02M062095.
    HGNCi HGNC:1617. CCT4.
    HPAi HPA029349.
    MIMi 605142. gene.
    neXtProti NX_P50991.
    PharmGKBi PA26181.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0459.
    HOGENOMi HOG000226735.
    HOVERGENi HBG106507.
    InParanoidi P50991.
    KOi K09496.
    OMAi PCAKMLV.
    OrthoDBi EOG722J8B.
    PhylomeDBi P50991.
    TreeFami TF106332.

    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 CCT4. human.
    GeneWikii CCT4.
    GenomeRNAii 10575.
    NextBioi 40137.
    PMAP-CutDB P50991.
    PROi P50991.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P50991.
    Bgeei P50991.
    CleanExi HS_CCT4.
    Genevestigatori P50991.

    Family and domain databases

    Gene3Di 1.10.560.10. 2 hits.
    3.30.260.10. 2 hits.
    3.50.7.10. 1 hit.
    InterProi IPR012717. Chap_CCT_delta.
    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 TIGR02342. chap_CCT_delta. 1 hit.
    PROSITEi PS00750. TCP1_1. 1 hit.
    PS00751. TCP1_2. 1 hit.
    PS00995. TCP1_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification of a group of cellular cofactors that stimulate the binding of RNA polymerase II and TRP-185 to human immunodeficiency virus 1 TAR RNA."
      Wu-Baer F., Lane W.S., Gaynor R.B.
      J. Biol. Chem. 271:4201-4208(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE.
    2. "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).
    3. "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: Brain and Thymus.
    4. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Brain.
    6. "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 2-8.
      Tissue: Platelet.
    7. Bienvenut W.V., Barblan J., Quadroni M.
      Submitted (MAR-2004) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 420-435, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: B-cell lymphoma.
    8. "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.
    9. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
      Tissue: Melanoma.
    10. "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-288; LYS-302; LYS-319 AND LYS-326, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "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.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiTCPD_HUMAN
    AccessioniPrimary (citable) accession number: P50991
    Secondary accession number(s): B2R6I3
    , B7Z8B1, F5H5W3, O14870, Q53QP9, Q96C51
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 140 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 2
      Human chromosome 2: 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