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P37802

- TAGL2_HUMAN

UniProt

P37802 - TAGL2_HUMAN

Protein

Transgelin-2

Gene

TAGLN2

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 150 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    GO - Molecular functioni

    1. protein binding Source: IntAct

    GO - Biological processi

    1. epithelial cell differentiation Source: UniProt

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Transgelin-2
    Alternative name(s):
    Epididymis tissue protein Li 7e
    SM22-alpha homolog
    Gene namesi
    Name:TAGLN2
    Synonyms:KIAA0120
    ORF Names:CDABP0035
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:11554. TAGLN2.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular vesicular exosome Source: UniProt
    2. vesicle Source: UniProtKB

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA36325.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 199198Transgelin-2PRO_0000204786Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine2 Publications
    Modified residuei17 – 171N6-acetyllysine1 Publication
    Modified residuei20 – 201N6-acetyllysine1 Publication
    Modified residuei163 – 1631Phosphoserine4 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP37802.
    PaxDbiP37802.
    PRIDEiP37802.

    2D gel databases

    DOSAC-COBS-2DPAGEP37802.
    OGPiP37802.
    REPRODUCTION-2DPAGEP37802.

    PTM databases

    PhosphoSiteiP37802.

    Expressioni

    Tissue specificityi

    Expressed in epididymis (at protein level).1 Publication

    Gene expression databases

    BgeeiP37802.
    CleanExiHS_TAGLN2.
    GenevestigatoriP37802.

    Organism-specific databases

    HPAiHPA001925.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ACTBP607093EBI-1056740,EBI-353944

    Protein-protein interaction databases

    BioGridi113995. 31 interactions.
    IntActiP37802. 12 interactions.
    MINTiMINT-5001664.
    STRINGi9606.ENSP00000357075.

    Structurei

    Secondary structure

    1
    199
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi24 – 3714
    Beta strandi38 – 403
    Helixi49 – 579
    Helixi60 – 6910
    Turni72 – 743
    Helixi86 – 10318
    Turni107 – 1093
    Helixi113 – 1175
    Helixi122 – 13615
    Beta strandi140 – 1423
    Beta strandi148 – 1514

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1WYMNMR-A16-157[»]
    ProteinModelPortaliP37802.
    SMRiP37802. Positions 9-158.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP37802.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini24 – 136113CHPROSITE-ProRule annotationAdd
    BLAST
    Repeati174 – 19926Calponin-likeAdd
    BLAST

    Sequence similaritiesi

    Belongs to the calponin family.Curated
    Contains 1 calponin-like repeat.PROSITE-ProRule annotation
    Contains 1 CH (calponin-homology) domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG5199.
    HOGENOMiHOG000232113.
    HOVERGENiHBG005186.
    InParanoidiP37802.
    OrthoDBiEOG718KD9.
    PhylomeDBiP37802.
    TreeFamiTF313921.

    Family and domain databases

    Gene3Di1.10.418.10. 1 hit.
    InterProiIPR000557. Calponin_repeat.
    IPR001715. CH-domain.
    IPR003096. SM22_calponin.
    IPR001061. TAGLN2.
    [Graphical view]
    PANTHERiPTHR18959:SF44. PTHR18959:SF44. 1 hit.
    PfamiPF00402. Calponin. 1 hit.
    PF00307. CH. 1 hit.
    [Graphical view]
    PRINTSiPR00888. SM22CALPONIN.
    SMARTiSM00033. CH. 1 hit.
    [Graphical view]
    SUPFAMiSSF47576. SSF47576. 1 hit.
    PROSITEiPS01052. CALPONIN_1. 1 hit.
    PS51122. CALPONIN_2. 1 hit.
    PS50021. CH. 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: P37802-1) [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

    MANRGPAYGL SREVQQKIEK QYDADLEQIL IQWITTQCRK DVGRPQPGRE    50
    NFQNWLKDGT VLCELINALY PEGQAPVKKI QASTMAFKQM EQISQFLQAA 100
    ERYGINTTDI FQTVDLWEGK NMACVQRTLM NLGGLAVARD DGLFSGDPNW 150
    FPKKSKENPR NFSDNQLQEG KNVIGLQMGT NRGASQAGMT GYGMPRQIL 199
    Length:199
    Mass (Da):22,391
    Last modified:January 23, 2007 - v3
    Checksum:i07DFC1652CE2383D
    GO
    Isoform 2 (identifier: P37802-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MSAFSLALALVSSPQPPPPIGM

    Note: No experimental confirmation available.

    Show »
    Length:220
    Mass (Da):24,454
    Checksum:iDD4502C038B8D6F6
    GO

    Sequence cautioni

    The sequence BAA04802.2 differs from that shown. Reason: Erroneous initiation.
    The sequence CAI14604.1 differs from that shown. Reason: Erroneous initiation.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti69 – 691L → Q.1 Publication
    Corresponds to variant rs17849636 [ dbSNP | Ensembl ].
    VAR_047903

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 11M → MSAFSLALALVSSPQPPPPI GM in isoform 2. 1 PublicationVSP_055311

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY007127 mRNA. Translation: AAG01993.1.
    D21261 mRNA. Translation: BAA04802.2. Different initiation.
    GU727636 mRNA. Translation: ADU87638.1.
    AK291562 mRNA. Translation: BAF84251.1.
    CR542126 mRNA. Translation: CAG46923.1.
    CR542136 mRNA. Translation: CAG46933.1.
    AL513485 Genomic DNA. Translation: CAI14603.1.
    AL513485 Genomic DNA. Translation: CAI14604.1. Different initiation.
    AL513485 Genomic DNA. Translation: CAI14602.1.
    CH471121 Genomic DNA. Translation: EAW52760.1.
    BC002616 mRNA. Translation: AAH02616.1.
    BC009357 mRNA. Translation: AAH09357.1.
    CCDSiCCDS1189.1. [P37802-1]
    CCDS60314.1. [P37802-2]
    RefSeqiNP_001264152.1. NM_001277223.1.
    NP_001264153.1. NM_001277224.1.
    NP_003555.1. NM_003564.2.
    UniGeneiHs.517168.

    Genome annotation databases

    EnsembliENST00000320307; ENSP00000357075; ENSG00000158710. [P37802-1]
    ENST00000368096; ENSP00000357076; ENSG00000158710. [P37802-2]
    ENST00000368097; ENSP00000357077; ENSG00000158710. [P37802-1]
    GeneIDi8407.
    KEGGihsa:8407.
    UCSCiuc001fun.2. human. [P37802-1]

    Polymorphism databases

    DMDMi586000.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY007127 mRNA. Translation: AAG01993.1 .
    D21261 mRNA. Translation: BAA04802.2 . Different initiation.
    GU727636 mRNA. Translation: ADU87638.1 .
    AK291562 mRNA. Translation: BAF84251.1 .
    CR542126 mRNA. Translation: CAG46923.1 .
    CR542136 mRNA. Translation: CAG46933.1 .
    AL513485 Genomic DNA. Translation: CAI14603.1 .
    AL513485 Genomic DNA. Translation: CAI14604.1 . Different initiation.
    AL513485 Genomic DNA. Translation: CAI14602.1 .
    CH471121 Genomic DNA. Translation: EAW52760.1 .
    BC002616 mRNA. Translation: AAH02616.1 .
    BC009357 mRNA. Translation: AAH09357.1 .
    CCDSi CCDS1189.1. [P37802-1 ]
    CCDS60314.1. [P37802-2 ]
    RefSeqi NP_001264152.1. NM_001277223.1.
    NP_001264153.1. NM_001277224.1.
    NP_003555.1. NM_003564.2.
    UniGenei Hs.517168.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1WYM NMR - A 16-157 [» ]
    ProteinModelPortali P37802.
    SMRi P37802. Positions 9-158.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113995. 31 interactions.
    IntActi P37802. 12 interactions.
    MINTi MINT-5001664.
    STRINGi 9606.ENSP00000357075.

    PTM databases

    PhosphoSitei P37802.

    Polymorphism databases

    DMDMi 586000.

    2D gel databases

    DOSAC-COBS-2DPAGE P37802.
    OGPi P37802.
    REPRODUCTION-2DPAGE P37802.

    Proteomic databases

    MaxQBi P37802.
    PaxDbi P37802.
    PRIDEi P37802.

    Protocols and materials databases

    DNASUi 8407.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000320307 ; ENSP00000357075 ; ENSG00000158710 . [P37802-1 ]
    ENST00000368096 ; ENSP00000357076 ; ENSG00000158710 . [P37802-2 ]
    ENST00000368097 ; ENSP00000357077 ; ENSG00000158710 . [P37802-1 ]
    GeneIDi 8407.
    KEGGi hsa:8407.
    UCSCi uc001fun.2. human. [P37802-1 ]

    Organism-specific databases

    CTDi 8407.
    GeneCardsi GC01M159887.
    HGNCi HGNC:11554. TAGLN2.
    HPAi HPA001925.
    MIMi 604634. gene.
    neXtProti NX_P37802.
    PharmGKBi PA36325.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5199.
    HOGENOMi HOG000232113.
    HOVERGENi HBG005186.
    InParanoidi P37802.
    OrthoDBi EOG718KD9.
    PhylomeDBi P37802.
    TreeFami TF313921.

    Miscellaneous databases

    ChiTaRSi TAGLN2. human.
    EvolutionaryTracei P37802.
    GeneWikii TAGLN2.
    GenomeRNAii 8407.
    NextBioi 31472.
    PROi P37802.
    SOURCEi Search...

    Gene expression databases

    Bgeei P37802.
    CleanExi HS_TAGLN2.
    Genevestigatori P37802.

    Family and domain databases

    Gene3Di 1.10.418.10. 1 hit.
    InterProi IPR000557. Calponin_repeat.
    IPR001715. CH-domain.
    IPR003096. SM22_calponin.
    IPR001061. TAGLN2.
    [Graphical view ]
    PANTHERi PTHR18959:SF44. PTHR18959:SF44. 1 hit.
    Pfami PF00402. Calponin. 1 hit.
    PF00307. CH. 1 hit.
    [Graphical view ]
    PRINTSi PR00888. SM22CALPONIN.
    SMARTi SM00033. CH. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47576. SSF47576. 1 hit.
    PROSITEi PS01052. CALPONIN_1. 1 hit.
    PS51122. CALPONIN_2. 1 hit.
    PS50021. CH. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Pediatric leukemia cDNA sequencing project."
      Zhou J., Yu W., Tang H., Mei G., Tsang Y.T.M., Bouck J., Gibbs R.A., Margolin J.F.
      Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Leukemia.
    2. "Prediction of the coding sequences of unidentified human genes. III. The coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by analysis of cDNA clones from human cell line KG-1."
      Nagase T., Miyajima N., Tanaka A., Sazuka T., Seki N., Sato S., Tabata S., Ishikawa K., Kawarabayasi Y., Kotani H., Nomura N.
      DNA Res. 2:37-43(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Bone marrow.
    3. "Systematic mapping and functional analysis of a family of human epididymal secretory sperm-located proteins."
      Li J., Liu F., Wang H., Liu X., Liu J., Li N., Wan F., Wang W., Zhang C., Jin S., Liu J., Zhu P., Liu Y.
      Mol. Cell. Proteomics 9:2517-2528(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
      Tissue: Epididymis.
    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] (ISOFORM 1).
      Tissue: Placenta.
    5. "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).
    6. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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), VARIANT GLN-69.
      Tissue: Lymph and Uterus.
    9. "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 2-12 (ISOFORMS 1/2).
      Tissue: Platelet.
    10. Bienvenut W.V., Claeys D.
      Submitted (FEB-2006) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-12; 41-57; 79-154 AND 161-196 (ISOFORMS 1/2), CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Platelet.
    11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-163, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Platelet.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "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].
    14. "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-163, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    15. "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-17 AND LYS-20, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "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-163, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "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-163, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "Solution structure of the CH domain of human transgelin-2."
      RIKEN structural genomics initiative (RSGI)
      Submitted (AUG-2005) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 16-157.

    Entry informationi

    Entry nameiTAGL2_HUMAN
    AccessioniPrimary (citable) accession number: P37802
    Secondary accession number(s): E9KL39
    , Q5JRQ6, Q5JRQ7, Q6FGI1, Q9BUH5, Q9H4P0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1994
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 150 of the entry and version 3 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

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3