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Q9UJW0

- DCTN4_HUMAN

UniProt

Q9UJW0 - DCTN4_HUMAN

Protein

Dynactin subunit 4

Gene

DCTN4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 102 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    Functioni

    Could have a dual role in dynein targeting and in ACTR1A/Arp1 subunit of dynactin pointed-end capping. Could be involved in ACTR1A pointed-end binding and in additional roles in linking dynein and dynactin to the cortical cytoskeleton.

    GO - Molecular functioni

    1. protein N-terminus binding Source: UniProtKB

    GO - Biological processi

    1. antigen processing and presentation of exogenous peptide antigen via MHC class II Source: Reactome

    Enzyme and pathway databases

    ReactomeiREACT_121399. MHC class II antigen presentation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dynactin subunit 4
    Short name:
    Dyn4
    Alternative name(s):
    Dynactin subunit p62
    Gene namesi
    Name:DCTN4
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:15518. DCTN4.

    Subcellular locationi

    Cytoplasmcytoskeleton 1 Publication. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome 1 Publication
    Note: In skeletal muscles, demonstrates a punctate distribution along costameres By similarity. Has a punctate cytoplasmic distribution as well as centrosomal distribution typical of dynactin. Overexpression does not disrupt microtubule organization or the integrity of the Golgi but does cause both cytosolic and nuclear distribution, suggesting that this polypeptide may be targeted to the nucleus at very high expression levels.By similarity

    GO - Cellular componenti

    1. centrosome Source: UniProtKB
    2. cytoplasm Source: ProtInc
    3. cytosol Source: Reactome
    4. dynactin complex Source: InterPro
    5. nucleus Source: ProtInc

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi30 – 301C → S: Loss of ATP7B-binding; when associated with S-33; S-51; S-54; S-70, S-73; S-76; S-79; S-111; S-114; S-277 and S-280. 1 Publication
    Mutagenesisi33 – 331C → S: Loss of ATP7B-binding; when associated with S-30; S-51; S-54; S-70, S-73; S-76; S-79; S-111; S-114; S-277 and S-280. 1 Publication
    Mutagenesisi51 – 511C → S: Loss of ATP7B-binding; when associated with S-30; S-33; S-54; S-70, S-73; S-76; S-79; S-111; S-114; S-277 and S-280. 1 Publication
    Mutagenesisi54 – 541C → S: Loss of ATP7B-binding; when associated with S-30; S-33; S-51; S-70, S-73; S-76; S-79; S-111; S-114; S-277 and S-280. 1 Publication
    Mutagenesisi70 – 701C → S: Loss of ATP7B-binding; when associated with S-30; S-33; S-51; S-54, S-73; S-76; S-79; S-111; S-114; S-277 and S-280. 1 Publication
    Mutagenesisi73 – 731C → S: Loss of ATP7B-binding; when associated with S-30; S-33; S-51; S-54, S-70; S-76; S-79; S-111; S-114; S-277 and S-280. 1 Publication
    Mutagenesisi76 – 761C → S: Loss of ATP7B-binding; when associated with S-30; S-33; S-51; S-54, S-70; S-73; S-79; S-111; S-114; S-277 and S-280. 1 Publication
    Mutagenesisi79 – 791C → S: Loss of ATP7B-binding; when associated with S-30; S-33; S-51; S-54, S-70; S-73; S-76; S-111; S-114; S-277 and S-280. 1 Publication
    Mutagenesisi111 – 1111C → S: Loss of ATP7B-binding; when associated with S-30; S-33; S-51; S-54, S-70; S-73; S-76; S-79; S-114; S-277 and S-280. 1 Publication
    Mutagenesisi114 – 1141C → S: Loss of ATP7B-binding; when associated with S-30; S-33; S-51; S-54, S-70; S-73; S-76; S-79; S-111; S-277 and S-280. 1 Publication
    Mutagenesisi277 – 2771C → S: Loss of ATP7B-binding; when associated with S-30; S-33; S-51; S-54, S-70; S-73; S-76; S-79; S-111; S-114 and S-280. 1 Publication
    Mutagenesisi280 – 2801C → S: Loss of ATP7B-binding; when associated with S-30; S-33; S-51; S-54, S-70; S-73; S-76; S-79; S-111; S-114 and S-277. 1 Publication

    Organism-specific databases

    Orphaneti586. Cystic fibrosis.
    PharmGKBiPA27183.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed3 Publications
    Chaini2 – 460459Dynactin subunit 4PRO_0000079823Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine3 Publications
    Modified residuei407 – 4071PhosphothreonineBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9UJW0.
    PaxDbiQ9UJW0.
    PeptideAtlasiQ9UJW0.
    PRIDEiQ9UJW0.

    PTM databases

    PhosphoSiteiQ9UJW0.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9UJW0.
    BgeeiQ9UJW0.
    CleanExiHS_DCTN4.
    GenevestigatoriQ9UJW0.

    Organism-specific databases

    HPAiCAB017532.

    Interactioni

    Subunit structurei

    Member of the pointed-end complex of the dynactin shoulder complex which contains DCTN4, DCTN5 and DCTN6 subunits and ACTR10 By similarity. Binds directly to the ACTR1A subunit of dynactin. Interacts with ATP7B, but not ATP7A, in a copper-dependent manner. Interacts with ANK2; this interaction is required for localization at costameres By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ANK2Q014841EBI-2134033,EBI-941975

    Protein-protein interaction databases

    BioGridi119345. 15 interactions.
    IntActiQ9UJW0. 9 interactions.
    MINTiMINT-4535396.
    STRINGi9606.ENSP00000414906.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9UJW0.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili152 – 17221Sequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Belongs to the dynactin subunit 4 family.Curated

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG147462.
    HOGENOMiHOG000007947.
    HOVERGENiHBG051324.
    InParanoidiQ9UJW0.
    KOiK10426.
    OMAiVGVFIKV.
    OrthoDBiEOG7SXW2X.
    PhylomeDBiQ9UJW0.
    TreeFamiTF105249.

    Family and domain databases

    InterProiIPR008603. Dynactin_p62.
    [Graphical view]
    PANTHERiPTHR13034. PTHR13034. 1 hit.
    PfamiPF05502. Dynactin_p62. 2 hits.
    [Graphical view]

    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: Q9UJW0-1) [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

    MASLLQSDRV LYLVQGEKKV RAPLSQLYFC RYCSELRSLE CVSHEVDSHY    50
    CPSCLENMPS AEAKLKKNRC ANCFDCPGCM HTLSTRATSI STQLPDDPAK 100
    TTMKKAYYLA CGFCRWTSRD VGMADKSVAS GGWQEPENPH TQRMNKLIEY 150
    YQQLAQKEKV ERDRKKLARR RNYMPLAFSD KYGLGTRLQR PRAGASISTL 200
    AGLSLKEGED QKEIKIEPAQ AVDEVEPLPE DYYTRPVNLT EVTTLQQRLL 250
    QPDFQPVCAS QLYPRHKHLL IKRSLRCRKC EHNLSKPEFN PTSIKFKIQL 300
    VAVNYIPEVR IMSIPNLRYM KESQVLLTLT NPVENLTHVT LFECEEGDPD 350
    DINSTAKVVV PPKELVLAGK DAAAEYDELA EPQDFQDDPD IIAFRKANKV 400
    GIFIKVTPQR EEGEVTVCFK MKHDFKNLAA PIRPIEESDQ GTEVIWLTQH 450
    VELSLGPLLP 460
    Length:460
    Mass (Da):52,337
    Last modified:May 1, 2000 - v1
    Checksum:i2105D6C0A713B11D
    GO
    Isoform 2 (identifier: Q9UJW0-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-57: Missing.

    Show »
    Length:403
    Mass (Da):45,757
    Checksum:i4919CE2359032038
    GO
    Isoform 3 (identifier: Q9UJW0-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         179-179: S → SQHTIHVV

    Show »
    Length:467
    Mass (Da):53,152
    Checksum:i2D4A445A6B764656
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti95 – 951P → T.1 Publication
    Corresponds to variant rs11550931 [ dbSNP | Ensembl ].
    VAR_054037
    Natural varianti263 – 2631Y → C.
    Corresponds to variant rs35772018 [ dbSNP | Ensembl ].
    VAR_033847
    Natural varianti342 – 3421F → L.1 Publication
    Corresponds to variant rs11954652 [ dbSNP | Ensembl ].
    VAR_024336
    Natural varianti438 – 4381S → N.
    Corresponds to variant rs3733923 [ dbSNP | Ensembl ].
    VAR_024337

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 5757Missing in isoform 2. 1 PublicationVSP_041306Add
    BLAST
    Alternative sequencei179 – 1791S → SQHTIHVV in isoform 3. CuratedVSP_041307

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF195120 mRNA. Translation: AAF03896.1.
    AK125973 mRNA. Translation: BAG54272.1.
    AK000299 mRNA. Translation: BAA91066.1.
    AC008450 Genomic DNA. No translation available.
    AC008453 Genomic DNA. No translation available.
    CH471062 Genomic DNA. Translation: EAW61706.1.
    CH471062 Genomic DNA. Translation: EAW61707.1.
    CH471062 Genomic DNA. Translation: EAW61709.1.
    BC026323 mRNA. Translation: AAH26323.1.
    CCDSiCCDS4310.1. [Q9UJW0-1]
    CCDS47310.1. [Q9UJW0-3]
    CCDS47311.1. [Q9UJW0-2]
    RefSeqiNP_001129115.1. NM_001135643.1. [Q9UJW0-3]
    NP_001129116.1. NM_001135644.1. [Q9UJW0-2]
    NP_057305.1. NM_016221.3. [Q9UJW0-1]
    UniGeneiHs.675564.

    Genome annotation databases

    EnsembliENST00000424236; ENSP00000411251; ENSG00000132912. [Q9UJW0-2]
    ENST00000446090; ENSP00000414906; ENSG00000132912. [Q9UJW0-3]
    ENST00000447998; ENSP00000416968; ENSG00000132912. [Q9UJW0-1]
    GeneIDi51164.
    KEGGihsa:51164.
    UCSCiuc003lsu.3. human. [Q9UJW0-1]
    uc010jhi.3. human. [Q9UJW0-3]

    Polymorphism databases

    DMDMi62900106.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF195120 mRNA. Translation: AAF03896.1 .
    AK125973 mRNA. Translation: BAG54272.1 .
    AK000299 mRNA. Translation: BAA91066.1 .
    AC008450 Genomic DNA. No translation available.
    AC008453 Genomic DNA. No translation available.
    CH471062 Genomic DNA. Translation: EAW61706.1 .
    CH471062 Genomic DNA. Translation: EAW61707.1 .
    CH471062 Genomic DNA. Translation: EAW61709.1 .
    BC026323 mRNA. Translation: AAH26323.1 .
    CCDSi CCDS4310.1. [Q9UJW0-1 ]
    CCDS47310.1. [Q9UJW0-3 ]
    CCDS47311.1. [Q9UJW0-2 ]
    RefSeqi NP_001129115.1. NM_001135643.1. [Q9UJW0-3 ]
    NP_001129116.1. NM_001135644.1. [Q9UJW0-2 ]
    NP_057305.1. NM_016221.3. [Q9UJW0-1 ]
    UniGenei Hs.675564.

    3D structure databases

    ProteinModelPortali Q9UJW0.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119345. 15 interactions.
    IntActi Q9UJW0. 9 interactions.
    MINTi MINT-4535396.
    STRINGi 9606.ENSP00000414906.

    PTM databases

    PhosphoSitei Q9UJW0.

    Polymorphism databases

    DMDMi 62900106.

    Proteomic databases

    MaxQBi Q9UJW0.
    PaxDbi Q9UJW0.
    PeptideAtlasi Q9UJW0.
    PRIDEi Q9UJW0.

    Protocols and materials databases

    DNASUi 51164.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000424236 ; ENSP00000411251 ; ENSG00000132912 . [Q9UJW0-2 ]
    ENST00000446090 ; ENSP00000414906 ; ENSG00000132912 . [Q9UJW0-3 ]
    ENST00000447998 ; ENSP00000416968 ; ENSG00000132912 . [Q9UJW0-1 ]
    GeneIDi 51164.
    KEGGi hsa:51164.
    UCSCi uc003lsu.3. human. [Q9UJW0-1 ]
    uc010jhi.3. human. [Q9UJW0-3 ]

    Organism-specific databases

    CTDi 51164.
    GeneCardsi GC05M150068.
    HGNCi HGNC:15518. DCTN4.
    HPAi CAB017532.
    MIMi 614758. gene.
    neXtProti NX_Q9UJW0.
    Orphaneti 586. Cystic fibrosis.
    PharmGKBi PA27183.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG147462.
    HOGENOMi HOG000007947.
    HOVERGENi HBG051324.
    InParanoidi Q9UJW0.
    KOi K10426.
    OMAi VGVFIKV.
    OrthoDBi EOG7SXW2X.
    PhylomeDBi Q9UJW0.
    TreeFami TF105249.

    Enzyme and pathway databases

    Reactomei REACT_121399. MHC class II antigen presentation.

    Miscellaneous databases

    GenomeRNAii 51164.
    NextBioi 54093.
    PROi Q9UJW0.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UJW0.
    Bgeei Q9UJW0.
    CleanExi HS_DCTN4.
    Genevestigatori Q9UJW0.

    Family and domain databases

    InterProi IPR008603. Dynactin_p62.
    [Graphical view ]
    PANTHERi PTHR13034. PTHR13034. 1 hit.
    Pfami PF05502. Dynactin_p62. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A dynactin subunit with a highly conserved cysteine-rich motif interacts directly with Arp1."
      Karki S., Tokito M.K., Holzbaur E.L.F.
      J. Biol. Chem. 275:4834-4839(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBUNIT, SUBCELLULAR LOCATION.
      Tissue: Neuron.
    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), VARIANT LEU-342.
      Tissue: Testis.
    3. "The DNA sequence and comparative analysis of human chromosome 5."
      Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
      , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
      Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT THR-95.
      Tissue: Brain.
    6. "Copper-dependent interaction of dynactin subunit p62 with the N terminus of ATP7B but not ATP7A."
      Lim C.M., Cater M.A., Mercer J.F., La Fontaine S.
      J. Biol. Chem. 281:14006-14014(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ATP7B, MUTAGENESIS OF CYS-30; CYS-33; CYS-51; CYS-54; CYS-70; CYS-73; CYS-76; CYS-79; CYS-111; CYS-114; CYS-277 AND CYS-280.
    7. "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], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "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 ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiDCTN4_HUMAN
    AccessioniPrimary (citable) accession number: Q9UJW0
    Secondary accession number(s): B3KWW0
    , D3DQH0, E5RGT5, Q8TAN8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 26, 2005
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 102 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 5
      Human chromosome 5: 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