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Q8TD16

- BICD2_HUMAN

UniProt

Q8TD16 - BICD2_HUMAN

Protein

Protein bicaudal D homolog 2

Gene

BICD2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 108 (01 Oct 2014)
      Sequence version 1 (01 Jun 2002)
      Previous versions | rss
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    Functioni

    May play a role in the dynein-dynactin interactions on the surface of membranous organelles, by associating with these complexes. Regulates coat complex coatomer protein I (COPI)-independent Golgi-endoplasmic reticulum transport by recruiting the dynein-dynactin motor complex By similarity.By similarity

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. Rab GTPase binding Source: BHF-UCL

    GO - Biological processi

    1. cell death Source: UniProtKB-KW
    2. microtubule anchoring at microtubule organizing center Source: BHF-UCL
    3. minus-end-directed organelle transport along microtubule Source: BHF-UCL

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein bicaudal D homolog 2
    Short name:
    Bic-D 2
    Gene namesi
    Name:BICD2
    Synonyms:KIAA0699
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:17208. BICD2.

    Subcellular locationi

    Golgi apparatus. Cytoplasmcytoskeleton
    Note: In interphase cells mainly localizes to the Golgi complex and colocalizes with dynactin at microtubule plus ends By similarity. Its localization is dependent on microtubule morphology.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. cytoplasmic vesicle Source: BHF-UCL
    3. cytoskeleton Source: UniProtKB-SubCell
    4. Golgi apparatus Source: HPA
    5. plasma membrane Source: HPA

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Golgi apparatus

    Pathology & Biotechi

    Involvement in diseasei

    Spinal muscular atrophy, lower extremity-predominant 2, autosomal dominant (SMALED2) [MIM:615290]: An autosomal dominant form of spinal muscular atrophy characterized by early-childhood onset of muscle weakness and atrophy predominantly affecting the proximal and distal muscles of the lower extremity, although some patients may show upper extremity involvement. The disorder results in delayed walking, waddling gait, difficulty walking, and loss of distal reflexes. Some patients may have foot deformities or hyperlordosis, and some show mild upper motor signs, such as spasticity. Sensation, bulbar function, and cognitive function are preserved. The disorder shows very slow progression throughout life.3 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti107 – 1071S → L in SMALED2; causes Golgi fragmentation; affects interaction with RAB6A and DNAI1 and the subcellular location of the protein. 3 Publications
    VAR_070112
    Natural varianti188 – 1881N → T in SMALED2; causes Golgi fragmentation. 1 Publication
    VAR_070113
    Natural varianti189 – 1891I → F in SMALED2. 1 Publication
    VAR_070114
    Natural varianti501 – 5011R → P in SMALED2; the mutation causes increased interaction with dynein; the mutant protein accumulates abnormally in the perinuclear region where it forms ring-like structures that colocalize with RAB6A. 1 Publication
    VAR_070115
    Natural varianti508 – 5081K → T in SMALED2. 1 Publication
    VAR_070116
    Natural varianti703 – 7031T → M in SMALED2; causes Golgi fragmentation. 1 Publication
    VAR_070117
    Natural varianti774 – 7741E → G in SMALED2; affects interaction with RAB6A and DNAI1 and the subcellular location of the protein. 1 Publication
    VAR_070118

    Keywords - Diseasei

    Disease mutation, Neurodegeneration

    Organism-specific databases

    MIMi615290. phenotype.
    Orphaneti363454. Autosomal dominant childhood-onset proximal spinal muscular atrophy with contractures.
    PharmGKBiPA134969018.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 824823Protein bicaudal D homolog 2PRO_0000205359Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine2 Publications
    Modified residuei190 – 1901Phosphoserine3 Publications
    Modified residuei224 – 2241Phosphoserine2 Publications
    Modified residuei343 – 3431Phosphoserine2 Publications
    Modified residuei395 – 3951Phosphoserine2 Publications
    Modified residuei582 – 5821Phosphoserine6 Publications
    Modified residuei821 – 8211Phosphothreonine2 Publications
    Modified residuei823 – 8231Phosphoserine2 Publications

    Post-translational modificationi

    Phosphorylated by NEK9 in vitro.7 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ8TD16.
    PaxDbiQ8TD16.
    PRIDEiQ8TD16.

    PTM databases

    PhosphoSiteiQ8TD16.

    Expressioni

    Tissue specificityi

    Ubiquitous.

    Gene expression databases

    BgeeiQ8TD16.
    CleanExiHS_BICD2.
    GenevestigatoriQ8TD16.

    Organism-specific databases

    HPAiHPA023013.
    HPA024452.

    Interactioni

    Subunit structurei

    Interacts with DCTN2 and RAB6A. Interacts with NEK9. Interacts with DNAI1.3 Publications

    Protein-protein interaction databases

    BioGridi116891. 13 interactions.
    DIPiDIP-53426N.
    IntActiQ8TD16. 8 interactions.
    MINTiMINT-5006473.
    STRINGi9606.ENSP00000349351.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8TD16.
    SMRiQ8TD16. Positions 716-797.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni663 – 803141Interacts with RAB6ABy similarityAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili20 – 269250Sequence AnalysisAdd
    BLAST
    Coiled coili338 – 537200Sequence AnalysisAdd
    BLAST
    Coiled coili666 – 808143Sequence AnalysisAdd
    BLAST

    Domaini

    The fourth coiled coil region is involved in Golgi targeting and in the interaction with DCTN2.By similarity

    Sequence similaritiesi

    Belongs to the BicD family.Curated

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG291306.
    HOVERGENiHBG050686.
    OMAiRNVLTNT.
    OrthoDBiEOG7BZVRK.
    PhylomeDBiQ8TD16.
    TreeFamiTF323833.

    Family and domain databases

    InterProiIPR018477. Bicaudal-D_microtubule-assoc.
    [Graphical view]
    PANTHERiPTHR31233. PTHR31233. 1 hit.
    PfamiPF09730. BicD. 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: Q8TD16-1) [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

    MSAPSEEEEY ARLVMEAQPE WLRAEVKRLS HELAETTREK IQAAEYGLAV    50
    LEEKHQLKLQ FEELEVDYEA IRSEMEQLKE AFGQAHTNHK KVAADGESRE 100
    ESLIQESASK EQYYVRKVLE LQTELKQLRN VLTNTQSENE RLASVAQELK 150
    EINQNVEIQR GRLRDDIKEY KFREARLLQD YSELEEENIS LQKQVSVLRQ 200
    NQVEFEGLKH EIKRLEEETE YLNSQLEDAI RLKEISERQL EEALETLKTE 250
    REQKNSLRKE LSHYMSINDS FYTSHLHVSL DGLKFSDDAA EPNNDAEALV 300
    NGFEHGGLAK LPLDNKTSTP KKEGLAPPSP SLVSDLLSEL NISEIQKLKQ 350
    QLMQMEREKA GLLATLQDTQ KQLEHTRGSL SEQQEKVTRL TENLSALRRL 400
    QASKERQTAL DNEKDRDSHE DGDYYEVDIN GPEILACKYH VAVAEAGELR 450
    EQLKALRSTH EAREAQHAEE KGRYEAEGQA LTEKVSLLEK ASRQDRELLA 500
    RLEKELKKVS DVAGETQGSL SVAQDELVTF SEELANLYHH VCMCNNETPN 550
    RVMLDYYREG QGGAGRTSPG GRTSPEARGR RSPILLPKGL LAPEAGRADG 600
    GTGDSSPSPG SSLPSPLSDP RREPMNIYNL IAIIRDQIKH LQAAVDRTTE 650
    LSRQRIASQE LGPAVDKDKE ALMEEILKLK SLLSTKREQI TTLRTVLKAN 700
    KQTAEVALAN LKSKYENEKA MVTETMMKLR NELKALKEDA ATFSSLRAMF 750
    ATRCDEYITQ LDEMQRQLAA AEDEKKTLNS LLRMAIQQKL ALTQRLELLE 800
    LDHEQTRRGR AKAAPKTKPA TPSL 824
    Length:824
    Mass (Da):93,533
    Last modified:June 1, 2002 - v1
    Checksum:i9C49138FF416378D
    GO
    Isoform 2 (identifier: Q8TD16-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         824-824: L → VSHTCACASDRAEGTGLANQVFCSEKHSIYCD

    Note: Due to intron retention. No experimental confirmation available.

    Show »
    Length:855
    Mass (Da):96,806
    Checksum:iDE52F8A0D1FCDFD8
    GO

    Sequence cautioni

    The sequence BAA31674.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti90 – 901K → R.1 Publication
    Corresponds to variant rs61754130 [ dbSNP | Ensembl ].
    VAR_070111
    Natural varianti107 – 1071S → L in SMALED2; causes Golgi fragmentation; affects interaction with RAB6A and DNAI1 and the subcellular location of the protein. 3 Publications
    VAR_070112
    Natural varianti188 – 1881N → T in SMALED2; causes Golgi fragmentation. 1 Publication
    VAR_070113
    Natural varianti189 – 1891I → F in SMALED2. 1 Publication
    VAR_070114
    Natural varianti501 – 5011R → P in SMALED2; the mutation causes increased interaction with dynein; the mutant protein accumulates abnormally in the perinuclear region where it forms ring-like structures that colocalize with RAB6A. 1 Publication
    VAR_070115
    Natural varianti508 – 5081K → T in SMALED2. 1 Publication
    VAR_070116
    Natural varianti703 – 7031T → M in SMALED2; causes Golgi fragmentation. 1 Publication
    VAR_070117
    Natural varianti774 – 7741E → G in SMALED2; affects interaction with RAB6A and DNAI1 and the subcellular location of the protein. 1 Publication
    VAR_070118

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei824 – 8241L → VSHTCACASDRAEGTGLANQ VFCSEKHSIYCD in isoform 2. 1 PublicationVSP_007969

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY052562 mRNA. Translation: AAL12246.1.
    AB014599 mRNA. Translation: BAA31674.1. Different initiation.
    AL137074, AL136981 Genomic DNA. Translation: CAI14369.1.
    AL137074, AL136981 Genomic DNA. Translation: CAI14370.1.
    AL136981, AL137074 Genomic DNA. Translation: CAI41013.1.
    AL136981, AL137074 Genomic DNA. Translation: CAI41014.1.
    BC004296 mRNA. Translation: AAH04296.1.
    BC073970 mRNA. Translation: AAH73970.1.
    CCDSiCCDS35064.1. [Q8TD16-2]
    CCDS6700.1. [Q8TD16-1]
    RefSeqiNP_001003800.1. NM_001003800.1. [Q8TD16-2]
    NP_056065.1. NM_015250.3. [Q8TD16-1]
    UniGeneiHs.436939.

    Genome annotation databases

    EnsembliENST00000356884; ENSP00000349351; ENSG00000185963. [Q8TD16-2]
    ENST00000375512; ENSP00000364662; ENSG00000185963. [Q8TD16-1]
    GeneIDi23299.
    KEGGihsa:23299.
    UCSCiuc004aso.1. human. [Q8TD16-1]
    uc004asp.1. human. [Q8TD16-2]

    Polymorphism databases

    DMDMi34098604.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY052562 mRNA. Translation: AAL12246.1 .
    AB014599 mRNA. Translation: BAA31674.1 . Different initiation.
    AL137074 , AL136981 Genomic DNA. Translation: CAI14369.1 .
    AL137074 , AL136981 Genomic DNA. Translation: CAI14370.1 .
    AL136981 , AL137074 Genomic DNA. Translation: CAI41013.1 .
    AL136981 , AL137074 Genomic DNA. Translation: CAI41014.1 .
    BC004296 mRNA. Translation: AAH04296.1 .
    BC073970 mRNA. Translation: AAH73970.1 .
    CCDSi CCDS35064.1. [Q8TD16-2 ]
    CCDS6700.1. [Q8TD16-1 ]
    RefSeqi NP_001003800.1. NM_001003800.1. [Q8TD16-2 ]
    NP_056065.1. NM_015250.3. [Q8TD16-1 ]
    UniGenei Hs.436939.

    3D structure databases

    ProteinModelPortali Q8TD16.
    SMRi Q8TD16. Positions 716-797.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116891. 13 interactions.
    DIPi DIP-53426N.
    IntActi Q8TD16. 8 interactions.
    MINTi MINT-5006473.
    STRINGi 9606.ENSP00000349351.

    PTM databases

    PhosphoSitei Q8TD16.

    Polymorphism databases

    DMDMi 34098604.

    Proteomic databases

    MaxQBi Q8TD16.
    PaxDbi Q8TD16.
    PRIDEi Q8TD16.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000356884 ; ENSP00000349351 ; ENSG00000185963 . [Q8TD16-2 ]
    ENST00000375512 ; ENSP00000364662 ; ENSG00000185963 . [Q8TD16-1 ]
    GeneIDi 23299.
    KEGGi hsa:23299.
    UCSCi uc004aso.1. human. [Q8TD16-1 ]
    uc004asp.1. human. [Q8TD16-2 ]

    Organism-specific databases

    CTDi 23299.
    GeneCardsi GC09M095473.
    HGNCi HGNC:17208. BICD2.
    HPAi HPA023013.
    HPA024452.
    MIMi 609797. gene.
    615290. phenotype.
    neXtProti NX_Q8TD16.
    Orphaneti 363454. Autosomal dominant childhood-onset proximal spinal muscular atrophy with contractures.
    PharmGKBi PA134969018.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG291306.
    HOVERGENi HBG050686.
    OMAi RNVLTNT.
    OrthoDBi EOG7BZVRK.
    PhylomeDBi Q8TD16.
    TreeFami TF323833.

    Miscellaneous databases

    GeneWikii BICD2.
    GenomeRNAii 23299.
    NextBioi 45128.
    PROi Q8TD16.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q8TD16.
    CleanExi HS_BICD2.
    Genevestigatori Q8TD16.

    Family and domain databases

    InterProi IPR018477. Bicaudal-D_microtubule-assoc.
    [Graphical view ]
    PANTHERi PTHR31233. PTHR31233. 1 hit.
    Pfami PF09730. BicD. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Purification, cloning, and characterization of Nek8, a novel NIMA-related kinase, and its candidate substrate Bicd2."
      Holland P.M., Milne A., Garka K., Johnson R.S., Willis C., Sims J.E., Rauch C.T., Bird T.A., Virca G.D.
      J. Biol. Chem. 277:16229-16240(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH NEK9, PHOSPHORYLATION BY NEK9.
    2. "Prediction of the coding sequences of unidentified human genes. X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
      Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 5:169-176(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Brain.
    3. "DNA sequence and analysis of human chromosome 9."
      Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
      , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
      Nature 429:369-374(2004) [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] OF 239-824 (ISOFORM 1).
      Tissue: Pancreas and Skin.
    5. "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 SER-582, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    6. "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-582, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    7. "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-190; SER-224; SER-343; SER-395 AND SER-582, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-190; THR-821 AND SER-823, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "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 SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    10. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    11. "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-582, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "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-582, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "Molecular defects in the motor adaptor BICD2 cause proximal spinal muscular atrophy with autosomal-dominant inheritance."
      Peeters K., Litvinenko I., Asselbergh B., Almeida-Souza L., Chamova T., Geuens T., Ydens E., Zimon M., Irobi J., De Vriendt E., De Winter V., Ooms T., Timmerman V., Tournev I., Jordanova A.
      Am. J. Hum. Genet. 92:955-964(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS SMALED2 LEU-107 AND GLY-774, CHARACTERIZATION OF VARIANTS SMALED2 LEU-107 AND GLY-774, INTERACTION WITH DNAI1 AND RAB6A.
    16. Cited for: VARIANTS SMALED2 LEU-107; PHE-189; PRO-501 AND THR-508, CHARACTERIZATION OF VARIANTS SMALED2 LEU-107 AND PRO-501, INTERACTION WITH DNAI1.
    17. Cited for: VARIANTS SMALED2 LEU-107; THR-188 AND MET-703, CHARACTERIZATION OF VARIANTS SMALED2 LEU-107; THR-188 AND MET-703, VARIANT ARG-90.

    Entry informationi

    Entry nameiBICD2_HUMAN
    AccessioniPrimary (citable) accession number: Q8TD16
    Secondary accession number(s): O75181
    , Q5TBQ2, Q5TBQ3, Q96LH2, Q9BT84, Q9H561
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 15, 2003
    Last sequence update: June 1, 2002
    Last modified: October 1, 2014
    This is version 108 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 9
      Human chromosome 9: 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