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P17987

- TCPA_HUMAN

UniProt

P17987 - TCPA_HUMAN

Protein

T-complex protein 1 subunit alpha

Gene

TCP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 155 (01 Oct 2014)
      Sequence version 1 (01 Nov 1990)
      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
    5. tubulin complex assembly 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 alpha
    Short name:
    TCP-1-alpha
    Alternative name(s):
    CCT-alpha
    Gene namesi
    Name:TCP1
    Synonyms:CCT1, CCTA
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:11655. TCP1.

    Subcellular locationi

    GO - Cellular componenti

    1. acrosomal vesicle Source: Ensembl
    2. cell body Source: Ensembl
    3. centrosome Source: MGI
    4. chaperonin-containing T-complex Source: Ensembl
    5. cytosol Source: Reactome
    6. extracellular vesicular exosome Source: UniProt
    7. Golgi apparatus Source: Ensembl
    8. microtubule Source: UniProtKB
    9. nuclear heterochromatin Source: Ensembl
    10. pericentriolar material Source: Ensembl
    11. zona pellucida receptor complex Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA36406.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 556556T-complex protein 1 subunit alphaPRO_0000128302Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine3 Publications
    Modified residuei181 – 1811Phosphotyrosine1 Publication
    Modified residuei182 – 1821Phosphothreonine1 Publication
    Modified residuei199 – 1991N6-acetyllysine1 Publication
    Modified residuei400 – 4001N6-acetyllysine1 Publication
    Modified residuei494 – 4941N6-acetyllysineBy similarity
    Modified residuei544 – 5441Phosphoserine4 Publications
    Modified residuei551 – 5511Phosphoserine2 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP17987.
    PaxDbiP17987.
    PeptideAtlasiP17987.
    PRIDEiP17987.

    2D gel databases

    OGPiP17987.
    REPRODUCTION-2DPAGEIPI00290566.
    P17987.
    UCD-2DPAGEP17987.

    PTM databases

    PhosphoSiteiP17987.

    Expressioni

    Gene expression databases

    ArrayExpressiP17987.
    BgeeiP17987.
    CleanExiHS_TCP1.
    GenevestigatoriP17987.

    Organism-specific databases

    HPAiCAB017460.
    HPA027337.
    HPA031082.

    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 CCT8.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    OLR1P783805EBI-356553,EBI-7151999

    Protein-protein interaction databases

    BioGridi112810. 91 interactions.
    DIPiDIP-33676N.
    IntActiP17987. 58 interactions.
    MINTiMINT-4999235.
    STRINGi9606.ENSP00000317334.

    Structurei

    3D structure databases

    ProteinModelPortaliP17987.
    SMRiP17987. Positions 2-534.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the TCP-1 chaperonin family.Curated

    Phylogenomic databases

    eggNOGiCOG0459.
    HOGENOMiHOG000226729.
    HOVERGENiHBG001052.
    InParanoidiP17987.
    KOiK09493.
    OMAiIMRIDTL.
    OrthoDBiEOG7K3TKJ.
    PhylomeDBiP17987.
    TreeFamiTF106331.

    Family and domain databases

    Gene3Di1.10.560.10. 2 hits.
    3.30.260.10. 2 hits.
    3.50.7.10. 1 hit.
    InterProiIPR017998. 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.
    PROSITEiPS00750. TCP1_1. 1 hit.
    PS00751. TCP1_2. 1 hit.
    PS00995. TCP1_3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P17987-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEGPLSVFGD RSTGETIRSQ NVMAAASIAN IVKSSLGPVG LDKMLVDDIG    50
    DVTITNDGAT ILKLLEVEHP AAKVLCELAD LQDKEVGDGT TSVVIIAAEL 100
    LKNADELVKQ KIHPTSVISG YRLACKEAVR YINENLIVNT DELGRDCLIN 150
    AAKTSMSSKI IGINGDFFAN MVVDAVLAIK YTDIRGQPRY PVNSVNILKA 200
    HGRSQMESML ISGYALNCVV GSQGMPKRIV NAKIACLDFS LQKTKMKLGV 250
    QVVITDPEKL DQIRQRESDI TKERIQKILA TGANVILTTG GIDDMCLKYF 300
    VEAGAMAVRR VLKRDLKRIA KASGATILST LANLEGEETF EAAMLGQAEE 350
    VVQERICDDE LILIKNTKAR TSASIILRGA NDFMCDEMER SLHDALCVVK 400
    RVLESKSVVP GGGAVEAALS IYLENYATSM GSREQLAIAE FARSLLVIPN 450
    TLAVNAAQDS TDLVAKLRAF HNEAQVNPER KNLKWIGLDL SNGKPRDNKQ 500
    AGVFEPTIVK VKSLKFATEA AITILRIDDL IKLHPESKDD KHGSYEDAVH 550
    SGALND 556
    Length:556
    Mass (Da):60,344
    Last modified:November 1, 1990 - v1
    Checksum:i486ECA836EA258A1
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti480 – 4801R → S in AAA61060. (PubMed:3653076)Curated
    Sequence conflicti537 – 5404SKDD → ILRI in CAA37064. (PubMed:2377466)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti7 – 71V → L in a breast cancer sample; somatic mutation. 1 Publication
    VAR_036258

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X52882 mRNA. Translation: CAA37064.1.
    BT006969 mRNA. Translation: AAP35615.1.
    AL135914 Genomic DNA. Translation: CAI21851.1.
    CH471051 Genomic DNA. Translation: EAW47616.1.
    CH471051 Genomic DNA. Translation: EAW47618.1.
    BC000665 mRNA. Translation: AAH00665.1.
    M26885 Genomic DNA. Translation: AAA61059.1.
    M27272, M26889 Genomic DNA. Translation: AAA61060.1.
    CCDSiCCDS5269.1.
    PIRiS10486.
    RefSeqiNP_110379.2. NM_030752.2.
    UniGeneiHs.363137.

    Genome annotation databases

    EnsembliENST00000321394; ENSP00000317334; ENSG00000120438.
    GeneIDi6950.
    KEGGihsa:6950.
    UCSCiuc003qsr.3. human.

    Polymorphism databases

    DMDMi135538.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X52882 mRNA. Translation: CAA37064.1 .
    BT006969 mRNA. Translation: AAP35615.1 .
    AL135914 Genomic DNA. Translation: CAI21851.1 .
    CH471051 Genomic DNA. Translation: EAW47616.1 .
    CH471051 Genomic DNA. Translation: EAW47618.1 .
    BC000665 mRNA. Translation: AAH00665.1 .
    M26885 Genomic DNA. Translation: AAA61059.1 .
    M27272 , M26889 Genomic DNA. Translation: AAA61060.1 .
    CCDSi CCDS5269.1.
    PIRi S10486.
    RefSeqi NP_110379.2. NM_030752.2.
    UniGenei Hs.363137.

    3D structure databases

    ProteinModelPortali P17987.
    SMRi P17987. Positions 2-534.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112810. 91 interactions.
    DIPi DIP-33676N.
    IntActi P17987. 58 interactions.
    MINTi MINT-4999235.
    STRINGi 9606.ENSP00000317334.

    PTM databases

    PhosphoSitei P17987.

    Polymorphism databases

    DMDMi 135538.

    2D gel databases

    OGPi P17987.
    REPRODUCTION-2DPAGE IPI00290566.
    P17987.
    UCD-2DPAGE P17987.

    Proteomic databases

    MaxQBi P17987.
    PaxDbi P17987.
    PeptideAtlasi P17987.
    PRIDEi P17987.

    Protocols and materials databases

    DNASUi 6950.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000321394 ; ENSP00000317334 ; ENSG00000120438 .
    GeneIDi 6950.
    KEGGi hsa:6950.
    UCSCi uc003qsr.3. human.

    Organism-specific databases

    CTDi 6950.
    GeneCardsi GC06M160199.
    HGNCi HGNC:11655. TCP1.
    HPAi CAB017460.
    HPA027337.
    HPA031082.
    MIMi 186980. gene.
    neXtProti NX_P17987.
    PharmGKBi PA36406.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0459.
    HOGENOMi HOG000226729.
    HOVERGENi HBG001052.
    InParanoidi P17987.
    KOi K09493.
    OMAi IMRIDTL.
    OrthoDBi EOG7K3TKJ.
    PhylomeDBi P17987.
    TreeFami TF106331.

    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 TCP1. human.
    GeneWikii T-complex_1.
    GenomeRNAii 6950.
    NextBioi 27215.
    PROi P17987.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P17987.
    Bgeei P17987.
    CleanExi HS_TCP1.
    Genevestigatori P17987.

    Family and domain databases

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

    Publicationsi

    1. "Nucleotide and amino-acid sequence of human testis-derived TCP1."
      Kirchhoff C., Willison K.R.
      Nucleic Acids Res. 18:4247-4247(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Testis.
    2. "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 (OCT-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    3. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. 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].
      Tissue: Colon.
    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 1-11, ACETYLATION AT MET-1.
      Tissue: Platelet.
    7. Lubec G., Vishwanath V.
      Submitted (MAR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 112-122; 131-145; 248-264; 469-480 AND 516-526, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Brain and Cajal-Retzius cell.
    8. "The human homologue of the mouse T-complex gene, TCP1, is located on chromosome 6 but is not near the HLA region."
      Willison K., Kelly A., Dudley K., Goodfellow P., Spurr N., Groves V., Gorman P., Sheer D., Trowsdale J.
      EMBO J. 6:1967-1974(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 308-365 AND 462-516.
    9. "T-complex polypeptide-1 is a subunit of a heteromeric particle in the eukaryotic cytosol."
      Lewis V.A., Hynes G.M., Zheng D., Saibil H., Willison K.R.
      Nature 358:249-252(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, SUBUNIT.
    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. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Platelet.
    13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-544, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. "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].
    15. "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 TYR-181; THR-182 AND SER-544, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    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 LYS-199 AND LYS-400, 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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-544 AND SER-551, 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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-544 AND SER-551, 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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    22. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    23. Cited for: VARIANT [LARGE SCALE ANALYSIS] LEU-7.

    Entry informationi

    Entry nameiTCPA_HUMAN
    AccessioniPrimary (citable) accession number: P17987
    Secondary accession number(s): E1P5B2, Q15556, Q5TCM3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1990
    Last sequence update: November 1, 1990
    Last modified: October 1, 2014
    This is version 155 of the entry and version 1 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 6
      Human chromosome 6: 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

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