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Q99832

- TCPH_HUMAN

UniProt

Q99832 - TCPH_HUMAN

Protein

T-complex protein 1 subunit eta

Gene

CCT7

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 145 (01 Oct 2014)
      Sequence version 2 (15 Jul 1998)
      Previous versions | rss
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    Functioni

    Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin By similarity.By similarity

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. 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 eta
    Short name:
    TCP-1-eta
    Alternative name(s):
    CCT-eta
    HIV-1 Nef-interacting protein
    Gene namesi
    Name:CCT7
    Synonyms:CCTH, NIP7-1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:1622. CCT7.

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA26185.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 543543T-complex protein 1 subunit etaPRO_0000128365Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine2 Publications
    Modified residuei67 – 671N6-acetyllysine1 Publication
    Modified residuei250 – 2501N6-acetyllysineBy similarity
    Modified residuei320 – 3201N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ99832.
    PaxDbiQ99832.
    PRIDEiQ99832.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00018465.

    PTM databases

    PhosphoSiteiQ99832.

    Expressioni

    Gene expression databases

    ArrayExpressiQ99832.
    BgeeiQ99832.
    CleanExiHS_CCT7.
    GenevestigatoriQ99832.

    Organism-specific databases

    HPAiHPA008425.

    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.1 Publication

    Protein-protein interaction databases

    BioGridi115825. 79 interactions.
    DIPiDIP-51608N.
    IntActiQ99832. 51 interactions.
    MINTiMINT-1131353.
    STRINGi9606.ENSP00000258091.

    Structurei

    3D structure databases

    ProteinModelPortaliQ99832.
    SMRiQ99832. Positions 6-523.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the TCP-1 chaperonin family.Curated

    Phylogenomic databases

    eggNOGiCOG0459.
    HOGENOMiHOG000226730.
    HOVERGENiHBG001052.
    InParanoidiQ99832.
    KOiK09499.
    OMAiCVWEPSI.
    OrthoDBiEOG7V49Z2.
    PhylomeDBiQ99832.
    TreeFamiTF105641.

    Family and domain databases

    Gene3Di1.10.560.10. 2 hits.
    3.30.260.10. 2 hits.
    3.50.7.10. 1 hit.
    InterProiIPR012720. Chap_CCT_eta.
    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:SF22. PTHR11353:SF22. 1 hit.
    PfamiPF00118. Cpn60_TCP1. 1 hit.
    [Graphical view]
    PRINTSiPR00304. TCOMPLEXTCP1.
    SUPFAMiSSF48592. SSF48592. 2 hits.
    SSF52029. SSF52029. 1 hit.
    TIGRFAMsiTIGR02345. chap_CCT_eta. 1 hit.
    PROSITEiPS00750. TCP1_1. 1 hit.
    PS00751. TCP1_2. 1 hit.
    PS00995. TCP1_3. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q99832-1) [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

    MMPTPVILLK EGTDSSQGIP QLVSNISACQ VIAEAVRTTL GPRGMDKLIV    50
    DGRGKATISN DGATILKLLD VVHPAAKTLV DIAKSQDAEV GDGTTSVTLL 100
    AAEFLKQVKP YVEEGLHPQI IIRAFRTATQ LAVNKIKEIA VTVKKADKVE 150
    QRKLLEKCAM TALSSKLISQ QKAFFAKMVV DAVMMLDDLL QLKMIGIKKV 200
    QGGALEDSQL VAGVAFKKTF SYAGFEMQPK KYHNPKIALL NVELELKAEK 250
    DNAEIRVHTV EDYQAIVDAE WNILYDKLEK IHHSGAKVVL SKLPIGDVAT 300
    QYFADRDMFC AGRVPEEDLK RTMMACGGSI QTSVNALSAD VLGRCQVFEE 350
    TQIGGERYNF FTGCPKAKTC TFILRGGAEQ FMEETERSLH DAIMIVRRAI 400
    KNDSVVAGGG AIEMELSKYL RDYSRTIPGK QQLLIGAYAK ALEIIPRQLC 450
    DNAGFDATNI LNKLRARHAQ GGTWYGVDIN NEDIADNFEA FVWEPAMVRI 500
    NALTAASEAA CLIVSVDETI KNPRSTVDAP TAAGRGRGRG RPH 543
    Length:543
    Mass (Da):59,367
    Last modified:July 15, 1998 - v2
    Checksum:i9F1E33FA80E6238E
    GO
    Isoform 2 (identifier: Q99832-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         3-89: Missing.
         90-206: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:339
    Mass (Da):37,499
    Checksum:iBA74E59CE7977306
    GO
    Isoform 3 (identifier: Q99832-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-44: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:499
    Mass (Da):54,804
    Checksum:i19F19C1820F6A80A
    GO
    Isoform 4 (identifier: Q99832-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         3-89: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:456
    Mass (Da):50,352
    Checksum:iAD52175094D0BD23
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti282 – 2832HH → RQ in AAB41437. 1 PublicationCurated
    Sequence conflicti293 – 2931L → P in AAB41437. 1 PublicationCurated
    Sequence conflicti336 – 3361A → P in AAB41437. 1 PublicationCurated
    Sequence conflicti364 – 3641C → L in AAB41437. 1 PublicationCurated
    Sequence conflicti374 – 3763LRG → SPC in AAB41437. 1 PublicationCurated
    Sequence conflicti407 – 4071A → P in AAB41437. 1 PublicationCurated
    Sequence conflicti411 – 4111A → P in AAB41437. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti259 – 2591T → A.
    Corresponds to variant rs2231427 [ dbSNP | Ensembl ].
    VAR_052269

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 4444Missing in isoform 3. 1 PublicationVSP_043572Add
    BLAST
    Alternative sequencei3 – 8987Missing in isoform 2 and isoform 4. 1 PublicationVSP_043573Add
    BLAST
    Alternative sequencei90 – 206117Missing in isoform 2. 1 PublicationVSP_043574Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF026292 mRNA. Translation: AAC96011.1.
    CR536511 mRNA. Translation: CAG38749.1.
    AK291961 mRNA. Translation: BAF84650.1.
    AK293597 mRNA. Translation: BAH11543.1.
    AK297846 mRNA. Translation: BAH12675.1.
    AK298153 mRNA. Translation: BAH12733.1.
    AC010913 Genomic DNA. Translation: AAX88902.1.
    CH471053 Genomic DNA. Translation: EAW99739.1.
    CH471053 Genomic DNA. Translation: EAW99740.1.
    BC019296 mRNA. Translation: AAH19296.1.
    BC088351 mRNA. Translation: AAH88351.1.
    U83843 mRNA. Translation: AAB41437.1.
    CCDSiCCDS42696.1. [Q99832-2]
    CCDS46336.1. [Q99832-1]
    CCDS54366.1. [Q99832-4]
    CCDS54367.1. [Q99832-3]
    RefSeqiNP_001009570.1. NM_001009570.2. [Q99832-2]
    NP_001159756.1. NM_001166284.1. [Q99832-4]
    NP_001159757.1. NM_001166285.1. [Q99832-3]
    NP_006420.1. NM_006429.3. [Q99832-1]
    UniGeneiHs.368149.

    Genome annotation databases

    EnsembliENST00000258091; ENSP00000258091; ENSG00000135624. [Q99832-1]
    ENST00000398422; ENSP00000381456; ENSG00000135624. [Q99832-2]
    ENST00000539919; ENSP00000437824; ENSG00000135624. [Q99832-3]
    ENST00000540468; ENSP00000442058; ENSG00000135624. [Q99832-4]
    GeneIDi10574.
    KEGGihsa:10574.
    UCSCiuc002siz.3. human. [Q99832-1]
    uc002sja.3. human. [Q99832-2]
    uc010yri.2. human. [Q99832-4]

    Polymorphism databases

    DMDMi3041738.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF026292 mRNA. Translation: AAC96011.1 .
    CR536511 mRNA. Translation: CAG38749.1 .
    AK291961 mRNA. Translation: BAF84650.1 .
    AK293597 mRNA. Translation: BAH11543.1 .
    AK297846 mRNA. Translation: BAH12675.1 .
    AK298153 mRNA. Translation: BAH12733.1 .
    AC010913 Genomic DNA. Translation: AAX88902.1 .
    CH471053 Genomic DNA. Translation: EAW99739.1 .
    CH471053 Genomic DNA. Translation: EAW99740.1 .
    BC019296 mRNA. Translation: AAH19296.1 .
    BC088351 mRNA. Translation: AAH88351.1 .
    U83843 mRNA. Translation: AAB41437.1 .
    CCDSi CCDS42696.1. [Q99832-2 ]
    CCDS46336.1. [Q99832-1 ]
    CCDS54366.1. [Q99832-4 ]
    CCDS54367.1. [Q99832-3 ]
    RefSeqi NP_001009570.1. NM_001009570.2. [Q99832-2 ]
    NP_001159756.1. NM_001166284.1. [Q99832-4 ]
    NP_001159757.1. NM_001166285.1. [Q99832-3 ]
    NP_006420.1. NM_006429.3. [Q99832-1 ]
    UniGenei Hs.368149.

    3D structure databases

    ProteinModelPortali Q99832.
    SMRi Q99832. Positions 6-523.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115825. 79 interactions.
    DIPi DIP-51608N.
    IntActi Q99832. 51 interactions.
    MINTi MINT-1131353.
    STRINGi 9606.ENSP00000258091.

    PTM databases

    PhosphoSitei Q99832.

    Polymorphism databases

    DMDMi 3041738.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00018465.

    Proteomic databases

    MaxQBi Q99832.
    PaxDbi Q99832.
    PRIDEi Q99832.

    Protocols and materials databases

    DNASUi 10574.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000258091 ; ENSP00000258091 ; ENSG00000135624 . [Q99832-1 ]
    ENST00000398422 ; ENSP00000381456 ; ENSG00000135624 . [Q99832-2 ]
    ENST00000539919 ; ENSP00000437824 ; ENSG00000135624 . [Q99832-3 ]
    ENST00000540468 ; ENSP00000442058 ; ENSG00000135624 . [Q99832-4 ]
    GeneIDi 10574.
    KEGGi hsa:10574.
    UCSCi uc002siz.3. human. [Q99832-1 ]
    uc002sja.3. human. [Q99832-2 ]
    uc010yri.2. human. [Q99832-4 ]

    Organism-specific databases

    CTDi 10574.
    GeneCardsi GC02P073460.
    HGNCi HGNC:1622. CCT7.
    HPAi HPA008425.
    MIMi 605140. gene.
    neXtProti NX_Q99832.
    PharmGKBi PA26185.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0459.
    HOGENOMi HOG000226730.
    HOVERGENi HBG001052.
    InParanoidi Q99832.
    KOi K09499.
    OMAi CVWEPSI.
    OrthoDBi EOG7V49Z2.
    PhylomeDBi Q99832.
    TreeFami TF105641.

    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 CCT7. human.
    GeneWikii CCT7.
    GenomeRNAii 10574.
    NextBioi 40131.
    PROi Q99832.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q99832.
    Bgeei Q99832.
    CleanExi HS_CCT7.
    Genevestigatori Q99832.

    Family and domain databases

    Gene3Di 1.10.560.10. 2 hits.
    3.30.260.10. 2 hits.
    3.50.7.10. 1 hit.
    InterProi IPR012720. Chap_CCT_eta.
    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:SF22. PTHR11353:SF22. 1 hit.
    Pfami PF00118. Cpn60_TCP1. 1 hit.
    [Graphical view ]
    PRINTSi PR00304. TCOMPLEXTCP1.
    SUPFAMi SSF48592. SSF48592. 2 hits.
    SSF52029. SSF52029. 1 hit.
    TIGRFAMsi TIGR02345. chap_CCT_eta. 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. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE 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; 2; 3 AND 4).
      Tissue: Cerebellum and Heart.
    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: PNS and Skin.
    7. Cited for: PROTEIN SEQUENCE OF 1-10; 56-67; 85-123; 127-144; 178-193; 200-217; 219-230; 237-247; 293-306; 314-320; 376-397; 402-418; 431-447 AND 500-535, ACETYLATION AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Colon carcinoma, Hepatoma and Osteosarcoma.
    8. Fukushi M., Kimura T., Yamamoto N.
      Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 13-424 (ISOFORM 1).
    9. Lubec G., Afjehi-Sadat L.
      Submitted (MAR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 107-123, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Brain and Cajal-Retzius cell.
    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. "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].
    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-67 AND LYS-320, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiTCPH_HUMAN
    AccessioniPrimary (citable) accession number: Q99832
    Secondary accession number(s): A8K7E6
    , A8MWI8, B7WNW9, B7Z4T9, B7Z4Z7, O14871, Q6FI26
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: July 15, 1998
    Last modified: October 1, 2014
    This is version 145 of the entry and version 2 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