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O43399

- TPD54_HUMAN

UniProt

O43399 - TPD54_HUMAN

Protein

Tumor protein D54

Gene

TPD52L2

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 134 (01 Oct 2014)
      Sequence version 2 (23 Jan 2002)
      Previous versions | rss
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    Functioni

    GO - Molecular functioni

    1. poly(A) RNA binding Source: UniProtKB
    2. protein binding Source: UniProtKB
    3. protein heterodimerization activity Source: UniProtKB
    4. protein homodimerization activity Source: UniProtKB

    GO - Biological processi

    1. regulation of cell proliferation Source: UniProtKB

    Enzyme and pathway databases

    SignaLinkiO43399.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tumor protein D54
    Short name:
    hD54
    Alternative name(s):
    Tumor protein D52-like 2
    Gene namesi
    Name:TPD52L2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 20

    Organism-specific databases

    HGNCiHGNC:12007. TPD52L2.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. perinuclear region of cytoplasm Source: UniProtKB

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA36688.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 206206Tumor protein D54PRO_0000185744Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine4 Publications
    Modified residuei3 – 31Phosphoserine2 Publications
    Modified residuei12 – 121Phosphoserine5 Publications
    Modified residuei19 – 191Phosphoserine1 Publication
    Modified residuei21 – 211Phosphoserine1 Publication
    Modified residuei96 – 961Phosphoserine3 Publications
    Modified residuei149 – 1491Phosphoserine1 Publication
    Modified residuei166 – 1661Phosphoserine7 Publications
    Modified residuei192 – 1921PhosphoserineBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiO43399.
    PaxDbiO43399.
    PRIDEiO43399.

    2D gel databases

    OGPiO43399.

    PTM databases

    PhosphoSiteiO43399.

    Expressioni

    Gene expression databases

    ArrayExpressiO43399.
    BgeeiO43399.
    CleanExiHS_TPD52L2.
    GenevestigatoriO43399.

    Organism-specific databases

    HPAiHPA047489.

    Interactioni

    Subunit structurei

    Forms a homodimer or heterodimer with other members of the family By similarity. Interacts with MAL2.By similarity1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Tpd52Q623932EBI-782616,EBI-782591From a different organism.

    Protein-protein interaction databases

    BioGridi113018. 47 interactions.
    IntActiO43399. 8 interactions.
    STRINGi9606.ENSP00000217121.

    Structurei

    3D structure databases

    ProteinModelPortaliO43399.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili38 – 8245Sequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Belongs to the TPD52 family.Curated

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG329468.
    HOGENOMiHOG000231968.
    HOVERGENiHBG058643.
    OMAiRARPFSH.
    OrthoDBiEOG744TBQ.
    PhylomeDBiO43399.
    TreeFamiTF317562.

    Family and domain databases

    InterProiIPR007327. TPD52.
    [Graphical view]
    PANTHERiPTHR19307. PTHR19307. 1 hit.
    PfamiPF04201. TPD52. 1 hit.
    [Graphical view]

    Sequences (7)i

    Sequence statusi: Complete.

    This entry describes 7 isoformsi produced by alternative splicing. Align

    Note: Additional isoforms seem to exist.

    Isoform 1 (identifier: O43399-1) [UniParc]FASTAAdd to Basket

    Also known as: HD54+ins2

    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

    MDSAGQDINL NSPNKGLLSD SMTDVPVDTG VAARTPAVEG LTEAEEEELR    50
    AELTKVEEEI VTLRQVLAAK ERHCGELKRR LGLSTLGELK QNLSRSWHDV 100
    QVSSAYVKTS EKLGEWNEKV TQSDLYKKTQ ETLSQAGQKT SAALSTVGSA 150
    ISRKLGDMRN SATFKSFEDR VGTIKSKVVG DRENGSDNLP SSAGSGDKPL 200
    SDPAPF 206
    Length:206
    Mass (Da):22,238
    Last modified:January 23, 2002 - v2
    Checksum:i58F01BC67B1E3DE9
    GO
    Isoform 2 (identifier: O43399-2) [UniParc]FASTAAdd to Basket

    Also known as: HD54-ins2

    The sequence of this isoform differs from the canonical sequence as follows:
         106-125: Missing.

    Show »
    Length:186
    Mass (Da):19,901
    Checksum:i002CD68479D8250C
    GO
    Isoform 3 (identifier: O43399-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         106-125: Missing.
         159-159: R → RAHPFSHSFSSYSIRHSISMPAMR

    Show »
    Length:209
    Mass (Da):22,517
    Checksum:i5087B635B9155443
    GO
    Isoform 4 (identifier: O43399-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         106-125: Missing.
         157-157: D → DMSSYSIRHSISMPA

    Show »
    Length:200
    Mass (Da):21,450
    Checksum:i9BAD0A523C8F14DB
    GO
    Isoform 5 (identifier: O43399-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         157-157: D → DMSSYSIRHSISMPA

    Note: No experimental confirmation available.

    Show »
    Length:220
    Mass (Da):23,787
    Checksum:i0A47C22C7C285FFF
    GO
    Isoform 6 (identifier: O43399-6) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         7-29: Missing.
         106-125: Missing.

    Show »
    Length:163
    Mass (Da):17,473
    Checksum:i1CF34D45DF97AABC
    GO
    Isoform 7 (identifier: O43399-7) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         157-157: D → DMRAHPFSHSFSSYSIRHSISMPA

    Note: No experimental confirmation available.

    Show »
    Length:229
    Mass (Da):24,854
    Checksum:i0AF18A6C7059BE30
    GO

    Sequence cautioni

    The sequence BU165202 differs from that shown. Reason: Frameshift at positions 155, 157, 173 and 188.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti72 – 721R → K in AAC98478. (PubMed:9838088)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei7 – 2923Missing in isoform 6. 1 PublicationVSP_045154Add
    BLAST
    Alternative sequencei106 – 12520Missing in isoform 2, isoform 3, isoform 4 and isoform 6. 1 PublicationVSP_006547Add
    BLAST
    Alternative sequencei157 – 1571D → DMSSYSIRHSISMPA in isoform 4 and isoform 5. 2 PublicationsVSP_038361
    Alternative sequencei157 – 1571D → DMRAHPFSHSFSSYSIRHSI SMPA in isoform 7. 1 PublicationVSP_047409
    Alternative sequencei159 – 1591R → RAHPFSHSFSSYSIRHSISM PAMR in isoform 3. CuratedVSP_036756

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF004429 mRNA. Translation: AAC98477.1.
    AF004430 mRNA. Translation: AAC98478.1.
    AK055068 mRNA. Translation: BAG51460.1.
    AK298366 mRNA. Translation: BAG60608.1.
    BT019631 mRNA. Translation: AAV38437.1.
    AL118506 Genomic DNA. Translation: CAC15492.1.
    AL118506 Genomic DNA. Translation: CAI21899.1.
    AL118506 Genomic DNA. Translation: CAI21900.1.
    AL118506 Genomic DNA. Translation: CAI21902.1.
    CH471077 Genomic DNA. Translation: EAW75195.1.
    CH471077 Genomic DNA. Translation: EAW75197.1.
    CH471077 Genomic DNA. Translation: EAW75198.1.
    CH471077 Genomic DNA. Translation: EAW75199.1.
    CH471077 Genomic DNA. Translation: EAW75201.1.
    BC006804 mRNA. Translation: AAH06804.1.
    BU165202 mRNA. No translation available.
    CCDSiCCDS13540.1. [O43399-1]
    CCDS13541.1. [O43399-2]
    CCDS13542.1. [O43399-7]
    CCDS13543.1. [O43399-3]
    CCDS13544.1. [O43399-5]
    CCDS13545.1. [O43399-4]
    CCDS58785.1. [O43399-6]
    RefSeqiNP_001230821.1. NM_001243892.1. [O43399-6]
    NP_003279.2. NM_003288.3. [O43399-1]
    NP_955392.1. NM_199360.2. [O43399-7]
    NP_955393.1. NM_199361.2. [O43399-3]
    NP_955394.1. NM_199362.2. [O43399-5]
    NP_955395.1. NM_199363.2. [O43399-4]
    UniGeneiHs.473296.

    Genome annotation databases

    EnsembliENST00000217121; ENSP00000217121; ENSG00000101150. [O43399-7]
    ENST00000346249; ENSP00000343547; ENSG00000101150. [O43399-1]
    ENST00000348257; ENSP00000343554; ENSG00000101150. [O43399-2]
    ENST00000351424; ENSP00000340006; ENSG00000101150. [O43399-3]
    ENST00000352482; ENSP00000344647; ENSG00000101150. [O43399-5]
    ENST00000358548; ENSP00000351350; ENSG00000101150. [O43399-4]
    ENST00000369927; ENSP00000358943; ENSG00000101150. [O43399-6]
    GeneIDi7165.
    KEGGihsa:7165.
    UCSCiuc002ygy.3. human.
    uc002ygz.3. human. [O43399-5]
    uc002yha.3. human. [O43399-3]
    uc002yhb.3. human. [O43399-4]
    uc002yhc.3. human. [O43399-1]
    uc011abl.2. human.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF004429 mRNA. Translation: AAC98477.1 .
    AF004430 mRNA. Translation: AAC98478.1 .
    AK055068 mRNA. Translation: BAG51460.1 .
    AK298366 mRNA. Translation: BAG60608.1 .
    BT019631 mRNA. Translation: AAV38437.1 .
    AL118506 Genomic DNA. Translation: CAC15492.1 .
    AL118506 Genomic DNA. Translation: CAI21899.1 .
    AL118506 Genomic DNA. Translation: CAI21900.1 .
    AL118506 Genomic DNA. Translation: CAI21902.1 .
    CH471077 Genomic DNA. Translation: EAW75195.1 .
    CH471077 Genomic DNA. Translation: EAW75197.1 .
    CH471077 Genomic DNA. Translation: EAW75198.1 .
    CH471077 Genomic DNA. Translation: EAW75199.1 .
    CH471077 Genomic DNA. Translation: EAW75201.1 .
    BC006804 mRNA. Translation: AAH06804.1 .
    BU165202 mRNA. No translation available.
    CCDSi CCDS13540.1. [O43399-1 ]
    CCDS13541.1. [O43399-2 ]
    CCDS13542.1. [O43399-7 ]
    CCDS13543.1. [O43399-3 ]
    CCDS13544.1. [O43399-5 ]
    CCDS13545.1. [O43399-4 ]
    CCDS58785.1. [O43399-6 ]
    RefSeqi NP_001230821.1. NM_001243892.1. [O43399-6 ]
    NP_003279.2. NM_003288.3. [O43399-1 ]
    NP_955392.1. NM_199360.2. [O43399-7 ]
    NP_955393.1. NM_199361.2. [O43399-3 ]
    NP_955394.1. NM_199362.2. [O43399-5 ]
    NP_955395.1. NM_199363.2. [O43399-4 ]
    UniGenei Hs.473296.

    3D structure databases

    ProteinModelPortali O43399.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113018. 47 interactions.
    IntActi O43399. 8 interactions.
    STRINGi 9606.ENSP00000217121.

    PTM databases

    PhosphoSitei O43399.

    2D gel databases

    OGPi O43399.

    Proteomic databases

    MaxQBi O43399.
    PaxDbi O43399.
    PRIDEi O43399.

    Protocols and materials databases

    DNASUi 7165.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000217121 ; ENSP00000217121 ; ENSG00000101150 . [O43399-7 ]
    ENST00000346249 ; ENSP00000343547 ; ENSG00000101150 . [O43399-1 ]
    ENST00000348257 ; ENSP00000343554 ; ENSG00000101150 . [O43399-2 ]
    ENST00000351424 ; ENSP00000340006 ; ENSG00000101150 . [O43399-3 ]
    ENST00000352482 ; ENSP00000344647 ; ENSG00000101150 . [O43399-5 ]
    ENST00000358548 ; ENSP00000351350 ; ENSG00000101150 . [O43399-4 ]
    ENST00000369927 ; ENSP00000358943 ; ENSG00000101150 . [O43399-6 ]
    GeneIDi 7165.
    KEGGi hsa:7165.
    UCSCi uc002ygy.3. human.
    uc002ygz.3. human. [O43399-5 ]
    uc002yha.3. human. [O43399-3 ]
    uc002yhb.3. human. [O43399-4 ]
    uc002yhc.3. human. [O43399-1 ]
    uc011abl.2. human.

    Organism-specific databases

    CTDi 7165.
    GeneCardsi GC20P062490.
    HGNCi HGNC:12007. TPD52L2.
    HPAi HPA047489.
    MIMi 603747. gene.
    neXtProti NX_O43399.
    PharmGKBi PA36688.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG329468.
    HOGENOMi HOG000231968.
    HOVERGENi HBG058643.
    OMAi RARPFSH.
    OrthoDBi EOG744TBQ.
    PhylomeDBi O43399.
    TreeFami TF317562.

    Enzyme and pathway databases

    SignaLinki O43399.

    Miscellaneous databases

    ChiTaRSi TPD52L2. human.
    GeneWikii TPD52L2.
    GenomeRNAii 7165.
    NextBioi 28048.
    PROi O43399.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O43399.
    Bgeei O43399.
    CleanExi HS_TPD52L2.
    Genevestigatori O43399.

    Family and domain databases

    InterProi IPR007327. TPD52.
    [Graphical view ]
    PANTHERi PTHR19307. PTHR19307. 1 hit.
    Pfami PF04201. TPD52. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning of a third member of the D52 gene family indicates alternative coding sequence usage in D52-like transcripts."
      Nourse C.R., Mattei M.-G., Gunning P., Byrne J.A.
      Biochim. Biophys. Acta 1443:155-168(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE SPLICING.
      Tissue: Mammary gland.
    2. "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 4 AND 6).
      Tissue: Brain and Kidney.
    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 (OCT-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
    4. "The DNA sequence and comparative analysis of human chromosome 20."
      Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
      , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
      Nature 414:865-871(2001) [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] (ISOFORMS 1 AND 7).
      Tissue: Placenta and Retinoblastoma.
    7. "Identification of MAL2, a novel member of the mal proteolipid family, though interactions with TPD52-like proteins in the yeast two-hybrid system."
      Wilson S.H.D., Bailey A.M., Nourse C.R., Mattei M.-G., Byrne J.A.
      Genomics 76:81-88(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MAL2.
    8. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12 AND SER-166, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
      Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
      J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-166, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: T-cell.
    10. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12 AND SER-166, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3; SER-12; SER-96 AND SER-166, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "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].
    13. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96; SER-149 AND SER-166, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    14. "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 MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12; SER-19; SER-21; SER-96 AND SER-166, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "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 MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3; SER-12 AND SER-166, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "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 MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiTPD54_HUMAN
    AccessioniPrimary (citable) accession number: O43399
    Secondary accession number(s): B4DPJ6
    , E1P5G7, O43398, Q5JWU5, Q5JWU6, Q5JWU8, Q5U0E0, Q9H3Z6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 24, 2001
    Last sequence update: January 23, 2002
    Last modified: October 1, 2014
    This is version 134 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, Reference proteome

    Documents

    1. Human chromosome 20
      Human chromosome 20: 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