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Q13561

- DCTN2_HUMAN

UniProt

Q13561 - DCTN2_HUMAN

Protein

Dynactin subunit 2

Gene

DCTN2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 143 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Modulates cytoplasmic dynein binding to an organelle, and plays a role in prometaphase chromosome alignment and spindle organization during mitosis. Involved in anchoring microtubules to centrosomes. May play a role in synapse formation during brain development.

    GO - Molecular functioni

    1. motor activity Source: UniProtKB-KW
    2. protein binding Source: UniProtKB
    3. spectrin binding Source: MGI

    GO - Biological processi

    1. antigen processing and presentation of exogenous peptide antigen via MHC class II Source: Reactome
    2. cell proliferation Source: UniProtKB
    3. G2/M transition of mitotic cell cycle Source: Reactome
    4. mitotic cell cycle Source: Reactome
    5. mitotic nuclear division Source: UniProtKB
    6. mitotic spindle organization Source: RefGenome

    Enzyme and pathway databases

    ReactomeiREACT_121399. MHC class II antigen presentation.
    REACT_15296. Recruitment of mitotic centrosome proteins and complexes.
    REACT_15364. Loss of Nlp from mitotic centrosomes.
    REACT_15451. Loss of proteins required for interphase microtubule organization from the centrosome.
    REACT_160315. Regulation of PLK1 Activity at G2/M Transition.
    SignaLinkiQ13561.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dynactin subunit 2
    Alternative name(s):
    50 kDa dynein-associated polypeptide
    Dynactin complex 50 kDa subunit
    Short name:
    DCTN-50
    p50 dynamitin
    Gene namesi
    Name:DCTN2
    Synonyms:DCTN50
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:2712. DCTN2.

    Subcellular locationi

    Cytoplasmcytoskeletonmicrotubule organizing centercentrosome 1 Publication. Membrane 1 Publication; Peripheral membrane protein 1 Publication

    GO - Cellular componenti

    1. centrosome Source: UniProtKB
    2. cytoplasm Source: HPA
    3. cytosol Source: Reactome
    4. dynactin complex Source: UniProtKB
    5. dynein complex Source: UniProtKB-KW
    6. extracellular vesicular exosome Source: UniProt
    7. growth cone Source: Ensembl
    8. kinetochore Source: UniProtKB
    9. membrane Source: UniProtKB-SubCell
    10. microtubule Source: UniProtKB-KW
    11. vesicle Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Dynein, Membrane, Microtubule

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA27181.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed3 Publications
    Chaini2 – 401400Dynactin subunit 2PRO_0000079821Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine2 Publications
    Modified residuei6 – 61Phosphotyrosine1 Publication
    Modified residuei83 – 831Phosphoserine1 Publication
    Modified residuei86 – 861PhosphotyrosineBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ13561.
    PaxDbiQ13561.
    PRIDEiQ13561.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00220503.

    PTM databases

    PhosphoSiteiQ13561.

    Miscellaneous databases

    PMAP-CutDBQ13561.

    Expressioni

    Gene expression databases

    ArrayExpressiQ13561.
    BgeeiQ13561.
    CleanExiHS_DCTN2.
    GenevestigatoriQ13561.

    Organism-specific databases

    HPAiHPA039715.
    HPA040040.

    Interactioni

    Subunit structurei

    Subunit of dynactin, a multiprotein complex associated with dynein. Interacts with BICD2 and CEP135 By similarity. Interacts with DYNAP, ECM29 and MAPRE1.By similarity3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    DISC1Q9NRI53EBI-715074,EBI-529989
    HTTP428586EBI-715074,EBI-466029

    Protein-protein interaction databases

    BioGridi115794. 52 interactions.
    IntActiQ13561. 24 interactions.
    MINTiMINT-206219.
    STRINGi9606.ENSP00000408910.

    Structurei

    3D structure databases

    ProteinModelPortaliQ13561.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili99 – 13234Sequence AnalysisAdd
    BLAST
    Coiled coili214 – 24431Sequence AnalysisAdd
    BLAST
    Coiled coili379 – 39921Sequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Belongs to the dynactin subunit 2 family.Curated

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG39555.
    HOVERGENiHBG051323.
    InParanoidiQ13561.
    KOiK10424.
    OMAiTQQMIAN.
    OrthoDBiEOG7JT6WG.
    PhylomeDBiQ13561.
    TreeFamiTF105247.

    Family and domain databases

    InterProiIPR028133. Dynamitin.
    [Graphical view]
    PANTHERiPTHR15346:SF0. PTHR15346:SF0. 1 hit.

    Sequences (3)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q13561-1) [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

    MADPKYADLP GIARNEPDVY ETSDLPEDDQ AEFDAEELTS TSVEHIIVNP    50
    NAAYDKFKDK RVGTKGLDFS DRIGKTKRTG YESGEYEMLG EGLGVKETPQ 100
    QKYQRLLHEV QELTTEVEKI KTTVKESATE EKLTPVLLAK QLAALKQQLV 150
    ASHLEKLLGP DAAINLTDPD GALAKRLLLQ LEATKNSKGG SGGKTTGTPP 200
    DSSLVTYELH SRPEQDKFSQ AAKVAELEKR LTELETAVRC DQDAQNPLSA 250
    GLQGACLMET VELLQAKVSA LDLAVLDQVE ARLQSVLGKV NEIAKHKASV 300
    EDADTQSKVH QLYETIQRWS PIASTLPELV QRLVTIKQLH EQAMQFGQLL 350
    THLDTTQQMI ANSLKDNTTL LTQVQTTMRE NLATVEGNFA SIDERMKKLG 400
    K 401
    Length:401
    Mass (Da):44,231
    Last modified:January 23, 2007 - v4
    Checksum:iC2FF01A9739337B2
    GO
    Isoform 2 (identifier: Q13561-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         35-35: A → AFAQEL

    Show »
    Length:406
    Mass (Da):44,820
    Checksum:i1166997A6D07479D
    GO
    Isoform 3 (identifier: Q13561-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         35-35: A → AEL

    Show »
    Length:403
    Mass (Da):44,473
    Checksum:i864FD68AF5433E22
    GO

    Sequence cautioni

    The sequence AAO34395.1 differs from that shown. Reason: Frameshift at position 381.

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei35 – 351A → AFAQEL in isoform 2. 2 PublicationsVSP_040485
    Alternative sequencei35 – 351A → AEL in isoform 3. 1 PublicationVSP_040486

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U50733 mRNA. Translation: AAC50423.1.
    AK314705 mRNA. Translation: BAG37252.1.
    AC022366 Genomic DNA. No translation available.
    AC022506 Genomic DNA. No translation available.
    BC000718 mRNA. Translation: AAH00718.1.
    BC009468 mRNA. Translation: AAH09468.1.
    BC014083 mRNA. Translation: AAH14083.1.
    AY189155 mRNA. Translation: AAO34395.1. Frameshift.
    CCDSiCCDS44930.1. [Q13561-2]
    CCDS58245.1. [Q13561-1]
    RefSeqiNP_001248341.1. NM_001261412.1. [Q13561-3]
    NP_001248342.1. NM_001261413.1. [Q13561-1]
    NP_006391.1. NM_006400.4. [Q13561-2]
    UniGeneiHs.289123.

    Genome annotation databases

    EnsembliENST00000434715; ENSP00000408910; ENSG00000175203. [Q13561-2]
    ENST00000548249; ENSP00000447824; ENSG00000175203. [Q13561-1]
    GeneIDi10540.
    KEGGihsa:10540.
    UCSCiuc001som.2. human. [Q13561-2]
    uc009zpv.2. human. [Q13561-1]

    Polymorphism databases

    DMDMi22096346.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U50733 mRNA. Translation: AAC50423.1 .
    AK314705 mRNA. Translation: BAG37252.1 .
    AC022366 Genomic DNA. No translation available.
    AC022506 Genomic DNA. No translation available.
    BC000718 mRNA. Translation: AAH00718.1 .
    BC009468 mRNA. Translation: AAH09468.1 .
    BC014083 mRNA. Translation: AAH14083.1 .
    AY189155 mRNA. Translation: AAO34395.1 . Frameshift.
    CCDSi CCDS44930.1. [Q13561-2 ]
    CCDS58245.1. [Q13561-1 ]
    RefSeqi NP_001248341.1. NM_001261412.1. [Q13561-3 ]
    NP_001248342.1. NM_001261413.1. [Q13561-1 ]
    NP_006391.1. NM_006400.4. [Q13561-2 ]
    UniGenei Hs.289123.

    3D structure databases

    ProteinModelPortali Q13561.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115794. 52 interactions.
    IntActi Q13561. 24 interactions.
    MINTi MINT-206219.
    STRINGi 9606.ENSP00000408910.

    PTM databases

    PhosphoSitei Q13561.

    Polymorphism databases

    DMDMi 22096346.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00220503.

    Proteomic databases

    MaxQBi Q13561.
    PaxDbi Q13561.
    PRIDEi Q13561.

    Protocols and materials databases

    DNASUi 10540.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000434715 ; ENSP00000408910 ; ENSG00000175203 . [Q13561-2 ]
    ENST00000548249 ; ENSP00000447824 ; ENSG00000175203 . [Q13561-1 ]
    GeneIDi 10540.
    KEGGi hsa:10540.
    UCSCi uc001som.2. human. [Q13561-2 ]
    uc009zpv.2. human. [Q13561-1 ]

    Organism-specific databases

    CTDi 10540.
    GeneCardsi GC12M057924.
    H-InvDB HIX0010763.
    HGNCi HGNC:2712. DCTN2.
    HPAi HPA039715.
    HPA040040.
    MIMi 607376. gene.
    neXtProti NX_Q13561.
    PharmGKBi PA27181.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG39555.
    HOVERGENi HBG051323.
    InParanoidi Q13561.
    KOi K10424.
    OMAi TQQMIAN.
    OrthoDBi EOG7JT6WG.
    PhylomeDBi Q13561.
    TreeFami TF105247.

    Enzyme and pathway databases

    Reactomei REACT_121399. MHC class II antigen presentation.
    REACT_15296. Recruitment of mitotic centrosome proteins and complexes.
    REACT_15364. Loss of Nlp from mitotic centrosomes.
    REACT_15451. Loss of proteins required for interphase microtubule organization from the centrosome.
    REACT_160315. Regulation of PLK1 Activity at G2/M Transition.
    SignaLinki Q13561.

    Miscellaneous databases

    ChiTaRSi DCTN2. human.
    GeneWikii DCTN2.
    GenomeRNAii 10540.
    NextBioi 39989.
    PMAP-CutDB Q13561.
    PROi Q13561.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q13561.
    Bgeei Q13561.
    CleanExi HS_DCTN2.
    Genevestigatori Q13561.

    Family and domain databases

    InterProi IPR028133. Dynamitin.
    [Graphical view ]
    PANTHERi PTHR15346:SF0. PTHR15346:SF0. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Molecular characterization of the 50-kD subunit of dynactin reveals function for the complex in chromosome alignment and spindle organization during mitosis."
      Echeverri C.J., Paschal B.M., Vaughan K.T., Vallee R.B.
      J. Cell Biol. 132:617-633(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PARTIAL PROTEIN SEQUENCE, SUBCELLULAR LOCATION.
    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] (ISOFORM 2).
    3. "The finished DNA sequence of human chromosome 12."
      Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
      , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
      Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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: Placenta, Skin and Uterus.
    5. "Human 50 kD dynactin subunit, p50 dynamitin, isolated from HeLa cells."
      Aumais J.P., Yu-Lee L.-Y.
      Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-385 (ISOFORM 3).
    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 2-14.
      Tissue: Platelet.
    7. Bienvenut W.V., Ramsay A., Leung H.Y.
      Submitted (FEB-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-14, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Embryonic kidney.
    8. Lubec G., Chen W.-Q., Sun Y.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 6-14; 79-96; 106-119; 157-185; 231-282 AND 366-395, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Fetal brain cortex.
    9. "The APC-associated protein EB1 associates with components of the dynactin complex and cytoplasmic dynein intermediate chain."
      Berrueta L., Tirnauer J.S., Schuyler S.C., Pellman D., Bierer B.E.
      Curr. Biol. 9:425-428(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MAPRE1.
    10. "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry."
      Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C.
      Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-6, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "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-83, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    13. "A protein interaction network for Ecm29 links the 26 S proteasome to molecular motors and endosomal components."
      Gorbea C., Pratt G., Ustrell V., Bell R., Sahasrabudhe S., Hughes R.E., Rechsteiner M.
      J. Biol. Chem. 285:31616-31633(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ECM29.
    14. "A novel human dynactin-associated protein, dynAP, promotes activation of Akt, and ergosterol-related compounds induce dynAP-dependent apoptosis of human cancer cells."
      Kunoh T., Noda T., Koseki K., Sekigawa M., Takagi M., Shin-ya K., Goshima N., Iemura S., Natsume T., Wada S., Mukai Y., Ohta S., Sasaki R., Mizukami T.
      Mol. Cancer Ther. 9:2934-2942(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DYNAP.
    15. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiDCTN2_HUMAN
    AccessioniPrimary (citable) accession number: Q13561
    Secondary accession number(s): B2RBK5, Q86YN2, Q9BW17
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 143 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 12
      Human chromosome 12: 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